How to Reduce Inflammation Naturally

Find out the difference between acute and chronic inflammation (one is good, one is bad). Also learn about the natural ways to reduce inflammation and improve your health through lifestyle, exercise, diet, and supplementation. 

Inflammation is one of those necessary evils. Yes, you need an inflammatory response in the body to alert you and your healing resources that something is wrong, and that is healthy inflammation. A twisted ankle, a reaction to stress, a bug or mosquito bite: these are common external examples of inflammation that let you know: you’ve hurt your ankle, you need a vacation, or it’s time to reapply the bug spray.

Unhealthy inflammation is chronic and persistent inflammation that is no longer helping you, only hurting. For instance if your ankle swells up so badly you can’t walk, you have to put ice on it, elevate it, maybe take an anti-inflammatory medication. But how do you reduce inflammation inside your body? You can’t ice your liver! Moreover how do you reduce inflammation naturally, without resorting to taking over-the-counter drugs and risking their side effects? Read on to find ways to reduce overall inflammation through lifestyle, diet, and natural supplements.

What Is Inflammation? Acute vs. Chronic

Acute inflammation is the immune system’s response to injury or foreign substance. It activates inflammation to deal with a specific threat, and then subsides. That inflammatory response includes the increased production of immune cells, cytokines, and white blood cells. The physical signs of acute inflammation are swelling, redness, pain, and heat. This is the healthy function of inflammation.

Chronic inflammation on the other hand is not beneficial to the body, and occurs when your immune system regularly and consistently releases inflammatory chemicals, even when there’s no injury to fix or foreign invader to fight.

To diagnosis chronic inflammation, doctors test for blood markers like interleukin-6 (IL-6), TNF alpha, homocysteine, and C-reactive protein (CRP). This type of inflammation often results from lifestyle factors such as poor diet, obesity, and stress, and is associated with many dangerous health conditions, including:

These are the conditions that can be caused or exacerbated by chronic inflammation, but what causes chronic inflammation itself? There are a few factors.

Habitually consuming high amounts of high-fructose corn syrup, sugar, refined carbs (like white bread), trans fats, and the vegetable oils included in so many processed foods is one contributor. Excessive alcohol intake is another culprit, and so is an inactive or sedentary lifestyle.

Now that you know what chronic inflammation is, where it comes from, and how it works, the final question is: how can you reduce chronic inflammation with natural remedies? Read on for the answers.

How to reduce inflammation naturally.

How to Reduce Inflammation Naturally Through Lifestyle, Diet, and Supplements

Here are several approaches you can take to combat inflammation naturally before resorting to over-the-counter drugs or medications.

Lifestyle Choices and Therapies to Fight Inflammation

Chronic inflammation is also called low-grade or systemic inflammation. There are some ways you can boost your health by managing lifestyle practices and fitness activities. Some practices you may want to adjust are as follows.

  • Avoid smoking
  • Limit alcohol consumption
  • Manage stress naturally (meditation perhaps, or tai chi)
  • Get sufficient sleep
  • Exercise regularly

When it comes to exercise, something as readily available as walking can help improve your health drastically, and when it comes to fitness with meditation, you could look into yoga. Those who practice yoga regularly have lower levels of the inflammatory marker IL-6, up to 41% lower than those who don’t practice yoga.

An Anti-Inflammatory Diet

A diet of anti-inflammatory foods is a huge component to reducing inflammation. As a general rule, you want to eat whole foods rather than processed foods, as they contain more nutrients and antioxidants for your health. Antioxidants help by reducing levels of free radicals in your body, molecules that cause cell damage and oxidative stress.

You’ll also want a healthy dietary balance between carbs, protein, fats, fruits, and veggies to ensure the proper amount of minerals, vitamins, and fiber throughout each day. One diet that’s been scientifically shown to have anti-inflammatory properties is the Mediterranean diet, which entails a high consumption of vegetables, along with olive oil and moderate amounts of lean protein.

Foods to Eat

Healthy eating can help you reduce inflammation in your body. These foods are the answer to how to reduce intestinal inflammation naturally. Reach inside and soothe what ails you!

  • High-fat fruits: Stone fruits like avocados and olives, including their oils
  • Whole grains: Whole grain wheat, barley, quinoa, oats, brown rice, spelt, rye, etc.
  • Vegetables: Leafy green and cruciferous vegetables especially, like kale, broccoli and broccoli greens, Brussels sprouts, cauliflower, and cabbage
  • Fruit: Dark berries like cherries and grapes particularly, either fresh or dried
  • Fatty fish: Salmon, anchovies, sardines, herring, and mackerel for omega-3 fatty acids
  • Nuts: Walnuts, almonds, cashews, Brazil nuts, etc.
  • Spices: Including turmeric, cinnamon, and fenugreek
  • Tea: Green tea especially
  • Red wine: Up to 10 ounces of red wine for men and 5 ounces for women per day
  • Peppers: Chili peppers and bell peppers of any color
  • Chocolate: Dark chocolate specifically, and the higher the cocoa bean percentage, the better

Foods to Avoid

These foods can help cause inflammation and amplify negative inflammatory effects in your body. You’d do well to reduce intake of or avoid entirely.

  • Alcohol: Hard liquors, beers, and ciders
  • Desserts: Candies, cookies, ice creams, and cakes
  • Processed meats: Sausages, hot dogs, and bologna
  • Trans fats: Foods containing partially hydrogenated ingredients like vegetable shortening, coffee creamer, ready-to-use frosting, and stick butter
  • Sugary beverages: Sugar-sweetened fruit juices, sports drinks, etc.
  • Refined carbs: White bread, white pasta, and white rice
  • Processed snacks: Crackers, pretzels, and chips
  • Certain oils and fried foods: Foods prepared with processed vegetable and seed oils like soybean oil, canola oil, corn oil, sunflower oil, etc.

When it comes to how to reduce liver inflammation naturally, what you avoid is just as important as what you put into your body, which is why it’s also recommended to quit smoking and avoid secondhand smoke and to limit your contact with toxic chemicals like aerosol cleaners.

Anti-Inflammatory Natural Supplements

You can help treat inflammation by including certain supplements that reduce inflammation.

Omega-3 Fatty Acids

Supplements like fish oil contain omega-3 fatty acids, and while eating fatty fish can also provide this nutrient, not everyone has the access or means to eat two to three helpings of fish per week.

Though both omega-3 and omega-6 fatty acids are essential to get from our diets, we often have a drastic overabundance of omega-6s and not nearly enough omega-3s to keep the ideal ratio between the two. Likewise, while red meat and dairy products may have anti-inflammatory effects, red meat and dairy are also prohibitive on certain diets and health care regimens (for example, red meat is not recommended for those with heart-health concerns). Supplementing with omega-3 fatty acids or fish oil can help defeat pro-inflammatory factors.

Herbs and Spices

Curcumin, found in the curry spice turmeric, has been shown to fight back against pro-inflammatory cytokines. And ginger also has been found to reduce inflammation even more successfully than NSAIDs (non-steroidal anti-inflammatory drugs) like aspirin, and with fewer side effects. Whether fresh or dried, certain herbs and spices can help reduce inflammation without having any detriment to your overall health.

Flame Off

With these tips, you can help reduce chronic inflammation in your life naturally, and the rewards for taking such precise care of yourself could be great. Those on an anti-inflammatory diet, for example, may find that certain health problems improve, from inflammatory bowel syndrome, to arthritis, to lupus and other autoimmune disorders. Not only that, but a healthier lifestyle leads almost invariably to lowered risk of developing chronic diseases like diabetes, heart disease, obesity, depression, and cancer. You’ll have better cholesterol, triglyceride, and blood sugar levels, plus an improvement in mood and energy. The bottom line is: lowering your levels of inflammation naturally increases your quality of life!

Muscle Atrophy: Causes, Treatment and Prevention

Learn about what causes muscle wasting or muscle atrophy, and how best to prevent and treat this condition, including through the use of physical therapy, medical intervention, and staying active. 

Muscle atrophy is essentially muscle wasting: it’s what happens when your muscles waste away, frequently as a result of a lack of physical activity. This article will explore the causes and symptoms of muscle atrophy, as well as preventative steps people can take if they’re immobile or bedridden due to illness. Loss of muscle mass or muscle strength can be particularly devastating for those who are already in positions of compromised health, and so in an effort to help you maintain your quality of life, we’ve compiled the relevant information here.

Muscle Atrophy: Definition

Atrophy of the muscles occurs when a person is inactive for so long that their skeletal muscles (these are the muscles attached to your bones which literally make your skeleton move) begin to break down, and the muscle protein is cannibalized by the body. This can happen in small instances or large, catastrophic instances.

Muscle atrophy of the hand or forearm may occur if you spend weeks in a cast to heal a broken arm, which is why people in casts are given exercises to do while they’re immobilized to prevent protein degradation in their muscles and muscle wasting. Muscle atrophy of the legs or muscle atrophy of the thighs can happen on a much larger scale to those who become wheelchair-bound, either temporarily or due to becoming permanently paraplegic. In even more extreme cases, those who have been held as prisoners of war may have full-body muscle wasting due to confinement and malnutrition for significantly long periods, sometimes years.

Muscle atrophy is a decrease in muscle mass, either partial or complete, which is most commonly suffered when a person becomes disabled or their movements severely restricted. This makes it difficult or impossible to move the part of the body where the muscle has atrophied, and medical advice should be sought for solutions.

Muscle atrophy: causes, treatment, and prevention.

Muscle Atrophy: Causes

Significant decreases in activity levels can lead to muscle atrophy, and there are many situations where that can occur, causing what’s known as disuse atrophy. There are also instances of muscle atrophy due to medical conditions that inhibit the use of a body part, and even rarer causes like the muscle atrophy experienced by astronauts after relatively short periods (a few days) of weightlessness. Muscle atrophy in situations of being bedbound or ceasing intense physical training can come on in as little as 2 weeks. Some of the other causes of muscle atrophy are as follows.

  • Lack of physical activity
  • Advanced aging
  • Malnutrition
  • Stroke
  • Alcohol-associated myopathy
  • Burns
  • Temporary disabling injuries (broken bones, torn rotator cuff)
  • Permanently disabling injuries (severed spinal cord, peripheral nerve damage)
  • Prolonged corticosteroid therapy

Some of the diseases and medical conditions that can disrupt or restrict movement, thus leading to muscle atrophy, include:

  • Spinal muscular atrophy: A hereditary wasting disease of the limbs.
  • Osteoarthritis: Degeneration of bones and joint cartilage that leads to decreased movement.
  • Polymyositis: An inflammatory disease of the muscles.
  • Amyotrophic lateral sclerosis (ALS or Lou Gehrig’s disease): Compromises the nerve cells of the spinal cord.
  • Muscular dystrophy: A hereditary disease that causes muscle weakness.
  • Multiple sclerosis (MS): An autoimmune disease that destroys the protective sheathing of brain and spinal nerves.
  • Rheumatoid arthritis (RA): A chronic inflammatory disease of the joints.
  • Dermatomyositis: Inflammation of the skin and underlying muscle tissue.
  • Polio: A virus afflicting muscle tissue, which can lead to paralysis.
  • Cancer cachexia: The weight loss, lack of energy, and loss of appetite in someone undergoing cancer treatment.
  • Guillain-Barré syndrome: An autoimmune disease and form of polyneuritis, which leads to paralysis of the limbs.
  • Neuropathy: Nerve damage that results in loss of sensation or functioning.

Muscle Atrophy: Symptoms

Regardless of the cause, these are the symptoms that may alert you to possible muscle atrophy, after which a trusted medical professional should be sought for advice.

  • One of your limbs (arms, legs) appears markedly smaller than the other one.
  • You’ve spent a long time physically inactive (bedridden, hospitalized).
  • You’re experiencing noticeable weakness in one limb.

Not to be flippant about the subject, but there is some truth to the phrase “use it or lose it” when it comes to muscle. If you cannot move your muscles with regular physical activity, you will start to lose them.

Muscle atrophy pain may or may not be a symptom, as that depends on the cause of the atrophy. Many people will begin to lose muscle before they are aware it’s happening, and will have to rely on visual muscle size to realize they need medical attention.

Muscle Atrophy: Diagnosis

Once you’ve gotten in contact with a medical professional, the diagnosis may involve your full medical history, a review of any previous injuries, as well as an evaluation of your symptoms. Diagnosing the atrophy may also involve diagnosing the underlying medical condition, which may require blood tests, X-rays, MRIs, CTs, a nerve conduction study, or a muscle and/or nerve biopsy to find out what could be causing muscle atrophy if it’s not readily apparently (as it would be if you’d suddenly become bedbound).

Can Muscle Atrophy Be Reversed?

Depending on the cause, yes. There are some cases where a proper diet, exercise, and physical therapy can not only reverse muscle atrophy, but also prevent it from recurring. However, this will not be the case in some disease-related forms of atrophy, and it is important that you consult your doctor on what your expectations for muscle atrophy recovery should be in restimulating protein synthesis and rebuilding your muscles.

Muscle Atrophy: Treatment

Again, this will depend on the diagnosis of the cause, and also the severity of your muscle loss, but the treatments for reversible muscle atrophy may be as follows.

  • Physical therapy
  • Exercise
  • Ultrasound therapy
  • Dietary changes
  • Surgery
  • Electrical stimulation

If a lack of movement caused this condition, regaining movement will go a long way towards fixing it, and moderate exercise like walking, along with physical therapy, may be a way to regain muscle strength without needing surgery to fix skin, tendons, or ligaments too tight to begin moving again (as in cases of contracture deformity that could be caused by malnutrition or burn injury scar tissue).

Muscle Atrophy: Prevention

There are ways to prevent muscle atrophy before it happens, and ways to guard against it if you were fortunate enough to recover your musculature after one instance of muscle loss. If preventing muscle atrophy is in your control (and, of course, sometimes it will not be), here are a few ways to maintain muscle strength in adverse circumstances.

Stay Active

If you’re in recovery from a severe illness or have just come home from the hospital after a debilitating accident, it’s not as if you’ll take up jogging right away. However, movements as small as walking to your mailbox each day, or around the block, or up and down a single flight of stairs, can truly make the difference in the long run when it comes to maintaining your mobility.

Stay Nourished

Depending on your condition, this may be difficult, but when your body lacks the proper nutrition to stay running, it will start to catabolize your muscles for its needs, which is a form of self-cannibalization or destructive metabolism that literally eats away at your muscles. Make sure you’re getting proper protein, if not from whole foods, then in the forms of protein shakes or supplements, as every little bit may help.

In fact, supplementing with amino acids has been proven to help accelerate muscle recovery in times of sickness and illness and can help boost your muscle-building gains. To learn more about amino acid therapy for muscle atrophy, give this informative article, written by one of the world’s foremost amino acid researchers, a read.

Seek Physical Therapy

Physical therapy is particularly valuable for those with severe injury recovery (such as a car crash survivor) or a neurological condition, as therapists provide professional guidance on what, and how, and how often to stretch your body to build strength.

Try Passive Movement

Another way physical therapy can help you even before you have the strength to help yourself is with passive movement. Passive movement requires the therapist to gently move your legs and arms for you. This is how you can begin to recover from a very deep muscle deficit and build up strength and muscle again.

Preventative Measures

Not only will the above advice help prevent muscle atrophy, but it can also help discourage bedsores in those who are bedridden due to illness, and reduce the chances of developing dangerous blood clots in the limbs. Likewise, these movements may prevent muscle stiffness, retraction, and nerve damage. Consult a medical professional or licensed physical therapist for more advice.

Eliminate Atrophy

If you are in danger of muscle atrophy, take steps to make sure your protein intake and nutrients are sufficient, including the use of a supplement if necessary, like Amino Co.’s essential amino acid supplement, which contains all of the essential aminos required to build new muscle cells and structures. Also, make sure that you stay active, no matter in how small a way, to preserve your muscle function and prevent your muscles from falling into complete disuse. You cannot always control your body’s condition, but if the type of atrophy you fear is the type that’s preventable, it’s well worth the effort to maintain the quality of life and movement you’ve come to expect.

What Are the Best Muscle Recovery Foods?

Wondering what muscle recovery foods are good for prevention and relief of delayed onset muscle soreness? This comprehensive list of foods full of healthy fats, amino acids, and natural sugars will support your workout and recovery goals.

After starting a new workout, you’re in for some growing pains. Delayed onset muscle soreness or DOMS can affect anyone, from those new to working out to elite athletes incorporating different exercises into their routines. Whenever you push your muscles, either with unfamiliar exercises or longer durations, you’re creating microscopic tears to the muscles, which then cause stiffness, soreness, and pain. Are sore muscles a good sign? Yes, in a sense, because it means you’re using your muscles in new ways that will eventually lead to a better fitness profile. But don’t fret! Eating muscle recovery foods can help ease the discomfort and may even help decrease muscle soreness in the first place.

Using food as your method of recovery and prevention may truly be the best road to take. The other suggestions to help muscle recovery either take extra time or come with other risks, and none of them can get in front of DOMS before it starts. Getting a massage after every workout would be great, but do you have the time, the money? Rest and ice packs are perfectly reasonable options too, but it’s the rest that might bother you if you’re really excited about a new workout and seeing results. Do you really want to take a couple of days off after every workout to let your muscles recover? It might not be a bad idea, but with the right foods pre- and post-workout, it might not be necessary either.

The last refuge to treat the ache and pain of muscle soreness is to use painkillers. Whether it’s over the counter fare you’d take for any pains (a wincing headache for example, or to relieve menstrual cramps), or prescription painkillers meant for more serious pains (a wrenched back or dental surgery). And these pain killers come with health-compromising side effects that are best avoided.

So what can you eat that will make a difference? Here are some foods you might want to include on the menu on gym days.

 Muscle recovery foods for prevention and relief.

Muscle Recovery Foods

Whether for their protein content, iron content, anti-inflammatory properties, or amino acids, these foods can help your muscles heal faster.

Cottage Cheese

Cottage cheese has around 27 grams of protein per cup, and is often a regular food in the fitness community for those without any dietary restrictions surrounding milk products. In fact, the casein protein found in cottage cheese curds (as opposed to the whey protein found in watery milk) are often isolated and used as a workout protein supplement. As a slow-digesting protein, casein can help build and rebuild muscle while you sleep if it’s your last snack before bed.

The essential amino acid leucine is also present in cottage cheese, and comprises around 23% of the essential amino acids in muscle protein (the most abundant percentage of them all). Foods with leucine can help you build muscle by activating protein synthesis, and the faster you rebuild your muscle, the faster your muscle repair and workout recovery!

Eat it plain, or combine cottage cheese with some of the other recovery foods on this list to stack the benefits. Cottage cheese can even be used in baked goods and pancakes or included in protein shakes—don’t be afraid to get creative.

Sweet Potatoes

Adding sweet potatoes to your post-workout meal can help replenish your glycogen stores after a tough workout. Sweet potatoes are a great source of vitamin C and beta-carotene as well, and are loaded with fiber which helps to control appetite and maintain healthy digestion and build muscle.

Sweet potatoes can be baked whole in the oven or on a grill, cut into fries, spiced with cinnamon, or made savory with garlic powder and pepper. Enjoy them at the dinner table or on the go: a baked potato wrapped in foil can join you just about anywhere.

Baking Spices

Speaking of what you can put on sweet potatoes, it turns out some baking spices are good for post-workout recovery as well. Not so much in the form of gingerbread cookies or cinnamon rolls, but a study showed that cinnamon or ginger given to 60 trained young women (between the ages of 13 and 25) significantly reduced their muscle soreness post-exercise. If you’re already having a sweet potato, make it a little sweeter with some cinnamon, add it to oatmeal, or put some in your coffee for the extra boost.

Coffee

Did we just mention coffee? Good news: coffee’s on the list too. Research suggests that about 2 cups of caffeinated coffee can reduce post-workout pain by 48%, and another study showed that pairing caffeine with painkilling pharmaceuticals resulted in a 40% reduction of the drugs taken. If you do need pharmaceutical pain relief, maybe coffee can help you minimize just how much you take—caffeine is a much less dangerous stimulant than pain pills.

Turmeric

Another spice on the list, turmeric contains the compound curcumin, which is an anti-inflammatory and an antioxidant, and has been shown to be a proven and reliable pain reliever. Whether it’s helping you with delayed onset muscle soreness or pain from an injury (workout-related or otherwise), turmeric eases both pain and swelling by blocking chemical pain messengers and pro-inflammatory enzymes.

As with the other spices, it can be easily added to baked goods, to coffee, and to oatmeal. With its beautiful golden color, you can even make what’s called “golden milk” or a turmeric latte by combining 2 cups of warm cow’s or almond milk with 1 teaspoon of turmeric and another teaspoon of ginger, and then sip your muscle soreness away.

Oatmeal

Speaking of oatmeal (and isn’t it nice that so many of these ingredients can be easily combined?), it, too, can help relieve muscle soreness. This complex carb gives you a slow and steady release of sugar, along with iron needed to carry oxygen through your blood, and vitamin B1 (thiamin), which can reduce stress and improve alertness. This is why oatmeal is a great way to start the day, but since it also includes selenium, a mineral that protects cells from free-radical damage and lowers the potential for joint inflammation, it’s a great food for those in high-intensity workout training as well (like, up to Olympic level training).

Use oatmeal as a daily vehicle for other healthy ingredients, including the spices on this list, and enjoy its reliable benefits.

Bananas

Easily sliced into oatmeal, included in smoothies, or eaten alone, not only are bananas a healthy way to replace sweets (frozen and blended they can even make a delicious ice cream alternative), bananas are also a great way to get much-needed potassium. Research suggests potassium helps reduce muscle soreness and muscle cramps like the dreaded “Charley horse” spasm that contracts your muscle against your will and might not let up until it causes enough damage to last for days. A banana a day could keep the Charley horse away, and is particularly delicious (and helpful) when paired with its classic mate: peanut butter.

Peanut Butter

The healthy fats and protein found in nut butters like peanut or almond butter can help repair sore muscles. A reliable source of protein for muscle building, with fiber for blood pressure aid, vitamin E for antioxidant properties, and phytosterols for heart health, peanut butter offers up a ton of benefit and is easy to eat anywhere. Make a sandwich, use it to help bind together portable protein balls filled with other ingredients, add it into smoothies, or just eat it from the jar with a spoon (no one’s judging).

Nuts and Seeds

If you’re a fan of protein balls, then you’re well acquainted with nuts and seeds, which are great additions to these protein-rich foods. While providing essential omega-3 fatty acids to fight inflammation, various nuts and seeds can provide you protein for muscle protein synthesis, electrolytes for hydration, and zinc for an immune system boost. Something as simple as a baggie full of almonds, walnuts, pumpkin, and cashews can help maximize your muscles. Mixing in seeds (sunflower, chia, pumpkin) adds a healthy density that can curb your hunger and satisfy your appetite for longer. They’re small but powerful assets in quick muscle recovery.

Manuka Honey

This is not your grocery store honey in its little bear- or hive-shaped bottle. Manuka honey comes from the Manuka bush in New Zealand, with a milder flavor than that of bee honey and a much thicker texture. It’s anti-inflammatory and rich in the carbs needed to replenish glycogen stores and deliver protein to your muscles. Drizzle it over yogurt or stir it into tea to gain its benefits.

Green Tea

Green tea is particularly helpful for muscle recovery purposes. With anti-inflammatory antioxidants, it makes an excellent pre- or post-workout drink to prevent muscle damage related to exercise, and also helps you stay hydrated.

Cacao

Cacao has high levels of magnesium, antioxidants, and B-vitamins, which reduce exercise stress, balance electrolytes, and boost immunity and energy levels. The antioxidant flavanols in cacao also help up the production of nitric oxide in your body, which allows your blood vessel walls to relax, lowering blood pressure and promoting healthy blood flow. Adding cacao powder to your high-quality protein shakes or a glass of cow/almond/coconut milk post-workout will bring you its benefits.

Tart Cherries

Tart cherry juice has been shown to minimize post-run muscle pain, reduce muscle damage, and improve recovery time in professional athletes like lifters, according to the Journal of the International Society of Sports Nutrition. Enjoy tart cherry juice as a drink, or include the dried fruit as a part of your own muscle-building trail mix with the nuts and seeds discussed above. It’s not the only fruit or fruit juice you might include either. The nutrients in fruits like oranges, pineapples, and raspberries can also help speed up your recovery.

Salmon

Rich with anti-inflammatory omega-3 fats, muscle-building protein, and antioxidants, salmon is an extremely efficient post-workout food. Not an option if you are vegan or vegetarian, of course, but for the meat eaters among us, or those on the Paleo diet, salmon can specifically help prevent delayed onset muscle soreness, reduce inflammation, and provide you with an abundance of the protein needed for muscle growth. Eat this protein within 45 minutes after working out for maximum effect, either grilled, cooked up in salmon cakes, or raw in the form of sushi or sashimi. All of the above goes for tuna as well, by the way—reasons you might become a pescatarian.

Eggs

If you are an omnivore or ovo-vegetarian, eggs are great way to gain protein first thing in the morning, and an even more effective food to have immediately post-workout to help prevent DOMS. Like cottage cheese, eggs are a rich provider of leucine, and like salmon, eggs contain vitamin D (in their yolks). For your convenience, eggs can be boiled and brought along for immediate consumption after your training. Boil a dozen at the start of each week during your meal prep, and have an easy protein source in the palm of your hand every other day of the week.

Spinach

Did we really get all the way to the end of the list without a vegetable? So sorry! Let’s fix that with spinach. A powerhouse of antioxidants, not only can spinach help prevent diseases like heart disease and various cancers, but it also helps you recover quickly from intense exercise. Spinach’s nitrates help to strengthen your muscles, and its magnesium content helps maintain nerve function. Spinach helps to regulate your blood sugar (in case you worry about the spikes you might get from the sweeter items on this list), and can be added to many dinners, snuck into smoothies, or eaten on its own either raw or sautéed in olive oil.

Resist Damage and Recovery Quickly

These foods help with recovery from DOMS and reduce the amount of soreness you get in the first place by providing your body with the proteins and nutrients it craves when you’re working out to the best of your ability.

A quick note before you go. In your quest for pain-free muscles, you’ll want to avoid:

  • Refined sugar: Just one sugary soda a day can increase your inflammatory markers, as can white bread and other products with refined sugar. Natural sugars don’t bring that kind of adverse effect, so get your sugar from whole foods instead.
  • Alcohol: The dehydration caused by alcohol requires its own special recovery, and will deplete many of your vitamins (especially B vitamins). Some research suggests that alcohol can interfere with how your body breaks down lactic acid, which would increase muscle soreness. If you’re on a mission to build muscle, it’s best to avoid alcohol.

If you’re eating pretty well and avoiding what you shouldn’t eat, but still find muscle soreness a burden after working out, there is always the option to supplement.

What is the best supplement for muscle recovery? Evidence shows that getting all your body’s essential amino acids in balance will help specifically with muscle sprains and pulls, so when supplementing, just make sure you cover the waterfront (rather than choosing one or two essentials and neglecting the rest). Other than that, a diverse diet can be had in choosing natural preventions and remedies for healthy muscle recovery.

How Amino Acids Support Female Muscle Growth

Is it truly more challenging for women to build muscle? To answer that question, we first separate the myths about gender differences and muscle growth from the actual science. Then, we offer tips everyone can use to get serious muscle growth results.

Female muscle growth. It’s not a phrase you hear too often. However, whether you’re a man or a woman, muscle building benefits your overall health and well-being. Strong scientific evidence shows that increasing your lean muscle mass can help you stay healthy as you age, support fat loss by keeping your metabolism running at full capacity and prevent the development of chronic diseases.

If you’re born male, you’re coached from a young age to want to grow up to be big and strong. But if you’re born female, you receive the opposite message. With the emergence of ripped and toned female fitness influencers taking social media by storm, the tides appear to be shifting. Nonetheless, society still tends to instruct girls to train themselves to be as dainty as possible—in part, so they can grow up to be women who attract big, strong men.

But the health benefits of muscle mass apply to everyone, regardless of gender. However, it can be more challenging for women to build muscle for a variety of reasons.

In this article, we’ll explore the scientific realities behind the common belief that muscle building comes more naturally to men than to women. Plus, we’ll offer tips that everyone can use to increase their physical strength and get serious muscle growth results.

Do Men Build Muscle More Easily Than Women?

If you’re at all familiar with the resources out there for people interested in muscle building, you’ve probably noticed that the vast majority of it is written by male authors for male audiences. While that has begun to shift somewhat as more women get into powerlifting, bodybuilding, and sports science, these realms are still dominated by men.

In those realms, a concept that many take for granted is that muscle gains come more easily for men than for women. This concept is propped up by claims that men and women have significant physiological differences that give men an advantage when it comes to physical strength and performance.

 

How amino acids can maximize female muscle growth.

What Science Tells Us About the Differences Between Men and Women

Let’s begin by comparing the average metabolic rates—the calories you burn just by going about your day—for men and women. According to a study published in the American Journal of Clinical Nutrition, about 90% of the variations researchers identified in the baseline number of calories participants expended over a 24-hour period came down to differences in fat mass and muscle mass. Your age has a measurable impact too. Researchers found that participants between 50 and 65 years of age had baseline metabolic rates that were 4.6% lower than participants between the ages of 20 and 30.

Fascinatingly, they reported: “No sex difference in any energy expenditure measurement could be found.” However, women do tend to have slower metabolisms than men, but it’s not because they’re women, it’s because on average, women are smaller and have less muscle mass.

So, let’s look into muscle mass differences. Findings published in the Journal of Applied Physiology reveal that women have, on average, about 67% of the muscle mass men do.

Women lag further behind when it comes to the muscle groups of the upper body than those of the lower body. A research team from the departments of Physical Education and Medicine at McMaster University in Hamilton, Canada set out to determine how gender differences influence strength and muscle fiber characteristics. They found that female participants had approximately 52% of the upper body strength and 66% of the lower body strength of men.

These differences appear to have more to do with the likelihood that men will have larger muscles than with innate sex-based differences, though. A study published in Ergonomics sought to measure the extent to which differences in strength between men and women can be explained by muscle size. Researchers found that when they adjusted their findings to take into account overall muscle mass as well as the size of specific muscle groups, 97% of sex-related differences were in strength. The researchers state that their findings suggest muscle size “almost entirely” accounts for the differences we expect to see between a man’s physical strength and a woman’s. In other words, if a man and woman have comparable muscle mass, they should be equally strong.

It appears that the vast majority of the differences we attribute to sex actually have to do with body composition. A woman and man with similar previous experience in terms of physical activity and comparative amounts of muscle and fat will perform similarly on standard measures of strength.

However, there are some differences between the ways men’s bodies and women’s bodies tend to respond to strength-training regimens and individual workout plans.

How Hormones Affect Female Muscle Growth

Hormones tend to be the first factor people point to when talking about physiological differences between women and men. It’s only logical, given that men’s increased muscle mass results from higher testosterone levels. Hormone levels fluctuate from person to person and over time, but on average, women produce far less testosterone than men do—between 15 and 20 times less, according to data sourced from the U.S. National Library of Medicine.

However, the question of testosterone levels isn’t as clear cut as we tend to think. In fact, some men have lower testosterone levels than some women do. After a team of researchers from the U.K. analyzed the hormone levels of elite athletes, they found significant overlap between testosterone levels for male competitors and female competitors. It’s worth noting that the hormone profiles of elite athletes differ from those of average individuals. It’s also highly likely that women with naturally higher levels of testosterone are more likely to excel at the elite level in certain physical disciplines. The main takeaway is that the idea that men have higher testosterone levels and therefore build new muscle more easily doesn’t entirely hold up.

Furthermore, did you know that testosterone is not the only hormone involved in building muscle mass? Estrogen, which as you may know, women typically produce at higher levels than men do, has also been shown to have significant benefits for muscle growth.

Studies done with animal subjects and well-controlled studies with human subjects support the idea that estrogen can help to prevent the breakdown of muscle tissue that often accompanies the aging process. It appears that estrogen has an overall positive impact when it comes to maintaining and increasing your lean muscle mass.

And an article published in Exercise and Sport Sciences Reviews presented experimental findings suggesting that estrogen may have an anabolic effect on muscles, meaning it supports muscle gain. It appears to do this primarily by lowering protein turnover, which slows the rate of catabolism (muscle breakdown), and enhancing the sensitivity of muscle tissue to resistance training.

Estrogen also boosts your metabolism, making it easier to cut your body fat percentage. While that doesn’t directly contribute to muscle growth, it does mean the new muscles you build will be more visible.

Women and Men Build Different Types of Muscles

We all have two general types of skeletal muscle fibers: slow-twitch, or Type 1, and fast-twitch, or Type 2. Type 1 muscles help power you through feats of endurance, like marathons. And the more Type 2 muscles you have, the better you perform on tests of explosive strength, like Olympic weight training.

There’s a clear divide between the average percentages of Type 1 and Type 2 muscle fibers that women and men typically have. According to Greg Nuckols, an experienced fitness writer who holds a BS in Exercise and Sports Science and three all-time world records for powerlifting, women typically have more Type 1 muscle fibers than men do, about 27% to 35% more. Women also tend to have greater capillary density.

Both give women an advantage in many ways. Greater capillary density means an increased ability to circulate blood through your muscle tissue to bring in fresh oxygen and clear out waste products. And having a higher percentage of Type 1 muscle fibers gives you an improved capacity for glucose and fatty acid oxidation, which translates to a decreased risk of chronic conditions linked to metabolic health, like diabetes and heart disease.

However, Type 2 muscle fibers are thicker, quicker to contract, and engage when your body nears maximum exertion. If you’re looking to increase your muscle mass and build strength so you can lift heavier and heavier weights, you need to recruit your Type 2 muscles. There’s no evidence that Type 1 muscle fibers can be transformed into Type 2 muscle fibers (or vice versa), which means there may always be a gap between the level of explosive strength an experienced female weight lifter can generate and the amount a male lifter at the same level can generate.

Maximizing Muscle Growth as a Woman

While men may have some innate advantages when it comes to building muscle mass, studies show that both men and women gain muscle at the same rate when they commit to workout routines like resistance training, weight training, and high-intensity interval training (HIIT).

Researchers from the University of Maryland Exercise Science and Wellness Research Laboratories conducted a study in which participants committed to a 6-month, whole-body strength-training program that worked for all the major muscle groups in both the upper and lower bodies.

They used MRI images to assess thigh and quadriceps muscle volume as well as mid-thigh muscle cross-sectional area before and after the strength-training program. Their findings showed that the thigh and quadriceps muscle volume increased significantly for all age and gender groups as a result of the strength-training program. The researchers found no significant differences related to either participant age or gender.

In some cases, women can make more significant strength and muscle gains than men. A study published in the International Journal of Sports Medicine examined how men and women responded to weight-training and resistance-training approaches. The researchers found that after following the same short-term training program, female participants made more significant strength increases than male participants did.

For women interested in optimizing their body composition by decreasing their body fat percentages and increasing their muscle mass, there are certain strategies you can put in place to maximize your muscle-building potential.

Train Strategically

When it comes to building muscle, the first step is to institute a strength-training regimen. For those seeking to rapidly increase muscle growth who are comfortable and able to perform high-intensity workouts, the most effective strength-training approach will involve lifting increasingly heavy weights. That might mean using barbell, kettlebells, dumbbells, or other types of weights.

Incorporating weightlifting into your training sessions encourages muscle growth because of the strain it places on your muscles. This wear and tear breaks down the muscle tissues. Then, during the recovery process that takes place while you sleep and on rest days, your muscles rebuild themselves. Each time this process takes place, your muscles grow bigger and stronger.

Adding high-intensity interval training to your exercise routine can also increase your muscle gains. This method of training involves short burst of intense exertion—a great tactic for recruiting your Type 2 muscles.

Increase Your Protein Intake

As you know, your muscles are made up of proteins. In order for your muscles to successfully rebuild themselves after workouts, you need to provide them with an adequate supply of dietary protein.

There’s no one-size-fits-all answer to the question of how much protein your muscles need to properly build and repair themselves. Factors like age, weight, activity level, and training goals will all influence the amount of protein an individual needs to consume.

Federal guidelines set the minimum recommended amount of protein consumption for adults at 17% to 21% of your daily calories, and that’s without taking weight training into consideration.

As Jim White, RD, ACSM, explained, resistance training increases the process of protein turnover. By eating proteins laden with all the essential amino acids, you’re providing your body with the raw materials it needs to build muscle.

According to the American College of Sports Medicine, if you’re looking to build muscle mass, you should aim to consume between 0.5 and 0.8 grams of protein per pound of body weight. That means a 150-pound woman, for example, should set a protein intake target of 75-120 grams of protein each day. It’s also important to consider the percentage of your overall calorie intake that comes from protein.

White, as well as other experts, recommends prioritizing the post-workout window for protein consumption as this has the biggest impact on muscle growth. Findings published in the Journal of the International Society of Sports Nutrition indicate that protein consumption before workouts can also be a key factor. Eating protein both before and after workouts can boost your performance, speed your recovery time, and increase your lean muscle mass.

Amino Acids Can Boost Female Muscle Growth

While it’s entirely possible to meet your body’s protein needs through diet alone, it can be helpful to add in high-quality supplements, including protein powders. Especially if you have a busy schedule that makes it challenging to consume enough protein during meal or snack times, it can be highly beneficial to provide your body with amino acids from other sources.

Researchers have found that certain supplements can be particularly helpful when it comes to building and maintaining muscle mass. If you’re wondering about the best amino acids for muscle growth, here are three to consider.

How amino acids can maximize female muscle growth.

1. Creatine

Creatine, an amino acid compound found naturally in the human body as well as in foods like red meat, has been the subject of hundreds of studies. If you’re lifting weights and looking to amplify your results, you may want to consider supplementing with creatine.

Media reports may have lead you to believe that creatine supplementation can adversely impact the health of your kidneys, but scientists have repeatedly and conclusively found that not to be the case.

After going over all available data on the short-, medium-, and long-term effects of creatine supplementation, researchers from the Higher Institute of Physical Education and Readaptation in Brussels, Belgium found no evidence that creatine causes liver dysfunction in healthy individuals (individuals with pre-existing kidney disease should avoid creatine). The researchers concluded that individuals who take creatine “do not report any adverse effects, but body mass increases.” They also noted that creatine may benefit the health of your heart and help reduce your risk of neurological diseases.

Studies show that supplementing with creatine can increase your lean body mass, enhance your anaerobic working capacity, and minimize the muscle damage caused by extreme exertion.

2. Beta-Alanine

This naturally occurring amino acid has also been the subject of extensive research.

One reason for this is that beta-alanine is the rate-limiting precursor of carnosine, an amino acid found in high concentrations in human skeletal muscle. One study on the effects of beta-alanine supplementation found that it can increase concentrations of carnosine in your muscles, which in turn helps to prevent muscular fatigue.

A separate study published in the Journal of the International Society of Sports Nutrition found pairing beta-alanine supplementation with high-intensity interval training (HIIT) can substantially increase both endurance and aerobic metabolism. It also showed a clear and impressive impact on subjects’ lean muscle mass.

Plus, a third study that examined how beta-alanine impacted anaerobic power output by using tests of physical strength such as timed sprints and a 90° bent-arm hang found that supplementing with beta-alanine improved participants’ results across all categories. Participants who supplemented with beta-alanine were able to achieve simultaneous weight loss and lean body mass increases.

3. Citrulline

Supplementing with citrulline can significantly increase your blood levels of not only this important amino acid, but two other crucial amino acids as well: ornithine and arginine. This can have a wide range of health benefits.

According to findings published in the The Journal of Strength & Conditioning Research, even a single dose of citrulline can improve your physical performance as measured by a flat barbell bench press. It can also reduce post-exercise muscle soreness. Participants were able to complete approximately 53% more repetitions and reported 40% less muscle soreness at both 24 and 48 hours afterward.

A separate study published in the British Journal of Sports Medicine showed that citrulline reduced muscular fatigue and improved muscle metabolism as measured by oxidative ATP production and the rate of phosphocreatine recovery after exercise.

All in all, it appears that this amino acid can improve endurance and speed up recovery time.

Greater Than the Sum of the Parts

Your muscles aren’t composed of single amino acids, but rather 20 separate amino acids. Building muscle mass requires a steady supply of all those amino acids. Nine of those are essential amino acids, meaning you must get them from the foods you eat or supplements you take.

While certain amino acids have been shown to have more dramatic results when it comes to muscle growth, your rate of muscle protein synthesis will be limited by whichever essential amino acid is in the shortest supply. That’s why some of the foremost experts on amino acids believe that taking an essential amino acid (EAA) blend is ultimately the most effective way to build your muscle mass. Using a supplement formulated to include all the required amino acid building blocks stimulates the production of new muscle tissue more effectively than any single amino acid could.

How to Use Amino Acids for Bodybuilding

Amino acids have become some of the most popular types of bodybuilding supplements across multiple disciplines. Both BCAAs and EAAs can be used on their own or in the form of “stacks”—specialized blends of multiple supplements that work together synergistically to provide even greater benefits than when taken on their own.

Bodybuilding usually refers to increasing and sculpting muscle mass for appearance as well as strength. In a more general sense, bodybuilding can refer to increasing muscle mass and function for the purpose of competing in sports such as football or power sports (e.qg., shot putting, discus throwing, etc.). It is a given that bodybuilding requires resistance training. If bodybuilding is for the purpose of improving competitive performance in a specific sport there are likely to be training requirements unique to that sport. This discussion on amino acids for bodybuilding will, therefore, not focus on the specific aspects of training. Regardless of the goal of training, amino acids play a key role in bodybuilding.

The Impact of Nutrition on Bodybuilding

Training tends to be the first factor most consider when seeking to build lean muscle, however, the nutrients we provide our bodies with can be equally influential—or more so—in determining how quickly we progress toward our goals. No matter how intensely you train, you will not be able to achieve the results you desire if you’re lacking certain crucial nutritional elements.

Obtaining all the nutrients you need from your diet alone in the quantities necessary for maximal bodybuilding results can be challenging. That’s where workout supplements come in.

By taking targeted sports nutrition supplements, you can ensure you get all the nutrients you need to build muscle, speed recovery time, decrease muscle soreness, amp up energy levels, and more.

Bodybuilding Supplements Then and Now

Depending on how broadly you interpret the idea of dietary supplementation, the idea of bodybuilding supplements can be traced back to ancient Greece.

According to Professor Andrew Dalby and other experts, Greek and Roman athletes consumed large quantities of meat and wine as well as herbal concoctions and tonics with the goal of increasing their strength and stamina.

In the early 1900s, Eugen Sandow, a pioneering German bodybuilder whose legacy earned him the honorific “father of modern bodybuilding,” advised all who wished to maximize their muscle growth to adhere to the dietary rules he himself followed. Bodybuilder Earle Liederman, who rose to prominence in the 1920s, recommended drinking what he called “beef juice” or “beef extract” (a substance the luminaries of today’s wellness landscape call “bone broth” and chefs simply refer to as “consommé) in order to speed muscle recovery.

In the 1950s, protein powders entered the picture as recreational and competitive bodybuilding became ever more popular with ever-broader audiences in the United States and elsewhere. Irvin P. Johnson, who operated a bodybuilding gym in Chicago, was one of the first to market egg-based protein powder. According to an article he published in Iron Man with the title “Build Bigger Biceps Faster with Food Supplements,” his specialized line of protein powders fueled serious strength gains. According to the article, he went from only being able to leg press 165 pounds for 10 repetitions to 660 pounds for 12 repetitions!

The bodybuilding supplement industry grew at an exponential rate throughout the 1970s and 1980s, fueled both by increased interest in recreational bodybuilding as well as advancements in advertising. Then, in October of 1994, Congress passed the Dietary Supplement Health and Education Act, a piece of legislation that transferred responsibility for determining the safety of dietary supplements such as protein powders and other mainstays of sports nutrition from the government to the manufacturers of the products. Unless they added a new dietary ingredient, manufacturers were no longer required to provide the U.S. Food and Drug Administration (FDA) with evidence to substantiate the safety or efficacy of their products. Legal experts believe this opened the door for the supplement industry to sell even more of their products. According to a Consumer Reports publication, annual sales of sports nutrition supplements hit $2.7 billion in 2010. And according to the “Sports Nutrition and High Energy Supplements – Global Market Outlook (2017-2026)” report sports nutrition and high energy supplements made $44.58 billion in 2017 with an outlook of $124.85 billion by 2026.

Defining the Term “Bodybuilding Supplements”

Just as the term bodybuilding can encompass both physique-focused and performance-focused endeavors, so too can the term “bodybuilding supplements” encompass a multitude of dietary supplements utilized by individuals engaged in bodybuilding as well as weight lifting, mixed martial arts, and other athletic pursuits to increase lean body mass as well as bring about other desirable outcomes such as:

  • Decreased body fat
  • Sharper muscle definition
  • Enhanced athletic performance

Amino acids have become some of the most popular types of bodybuilding supplements across multiple disciplines. Both branched-chain amino acid supplements (BCAA supplements) and essential amino acids (EAAs) can be used on their own or in the form of “stacks”—specialized blends of multiple supplements that work together synergistically to provide even greater benefits than when taken on their own.

Making the Most of the Building Blocks of Protein

Amino acids have earned the nickname “the building blocks protein” because of the vital role they play in creating muscle tissue. While it’s certainly possible to obtain all the amino acids you need simply by eating high-protein foods like eggs, lean meats, legumes, vegetables, and pseudo-grains like quinoa, amino acid supplements can be a convenient and efficient way to maximize the benefits of amino acids.

One of the most compelling reasons to use supplements can be captured in a single word: bioavailability. Bioavailability refers to how efficiently a substance can be metabolized and the percentage of what’s ingested that’s utilized for its intended purpose inside the body.

Several factors determine the bioavailability of each amino acid. For example, when taking in amino acids from a food source, the amount of fat contained in that food influences the length of time it takes for amino acids to be put to use. The way you cook food can also impact the amino acids it contains. Some heat-sensitive amino acids can even decompose when cooked. And not all amino acid supplements are metabolized at the same rate. The physical nature of the supplement will have the most significant influence on its bioavailability. A BCAA powder, for instance, will be digested differently than a supplement in pill or liquid form. The extent to which a supplement is pre-digested as well as whether it contains any fillers or binders impact its overall bioavailability.

Understanding Muscle Protein Turnover

Muscle protein turnover is the metabolic basis that powers increased muscle mass, strength, and function.

Muscle protein turnover refers to the constant breakdown of older muscle proteins that are no longer operating at peak efficiency and their replacement with newly synthesized, more efficient muscle protein fibers. The balance between protein synthesis and breakdown determines whether a muscle is growing or shrinking.

Muscle function is accomplished by the contraction of muscle protein fibers. Muscle strength and function are determined by how many muscle protein fibers you have and the efficiency with which they contract. Increasing muscle protein mass and contractile efficiency is accomplished by optimizing muscle protein turnover.

For bodybuilding, the goal is to make the rate of muscle protein synthesis exceed the rate of protein breakdown. Further, the increased balance between muscle protein synthesis and breakdown should optimally be accomplished mainly by stimulating synthesis, not lessening breakdown—protein breakdown gets rid of muscle proteins that are not functioning efficiently, so it is good to keep that process functioning at full speed.

The Mechanics of Muscle Protein Synthesis

Muscle proteins are composed of a series of amino acids hooked together in a specific order determined by the messenger RNA (mRNA) in the cell for each specific muscle protein. The sequence of the mRNA is dictated by the DNA in the cell. There is a specific molecule for each amino acid (tRNA) that delivers it to the mRNA as required for incorporation into the protein that is being produced.

A simple, conceptual way to think about the process of muscle protein synthesis is to compare it to the construction of a building. The DNA is basically the idea for the design of the building. The RNA is the written plan or blueprint, and transcription of the mRNA from the DNA is the process of writing up the plan. The tRNA molecules that bring the amino acids to the mRNA for incorporation into protein are like trucks that bring bricks to the building site, and the hooking of amino acids together in the proper order on the mRNA corresponds to the builder putting the bricks together according to the blueprint. The protein is the final product, or completed building, ready to serve its function.

The details of how muscle protein is made are important only so that it is clear why all the amino acids must be available in abundance. If the mRNA dictates that the next amino acid in the chain making up the protein is a particular amino acid that is deficient, then the process is halted and no muscle protein is produced.

How Amino Acids Impact Muscle Protein Synthesis

We must derive certain amino acids, as I touched on earlier, from dietary protein. However, the human body can synthesize other amino acids through chemical reactions that occur in the liver and select sites throughout the body.

The amino acids that must be obtained from the diet are called essential amino acids, or EAAs, while the amino acids that can be made in the body are called nonessential amino acids, or NEAAS.

The nine essential amino acids are leucine, isoleucine, valine, phenylalanine, lysine, methionine, phenylalanine, threonine, and tryptophan. Three of the EAAs, leucine, isoleucine, and valine, have been subcategorized as branched-chain amino acids (BCAAs), a descriptor which refers to their chemical structure. We typically put the number of nonessential amino acids at 11, as that’s how many NEAAs can be found in human protein, though other NEAAs like citrulline and ornithine can be found elsewhere in the body.

Since your body can produce NEAAS and they are available in abundance, the availability of EAAs serves as the limiting factor for setting the rate of muscle protein synthesis.

Using Essential Amino Acids to Stimulate Muscle Growth

Consuming essential amino acids, either as dietary protein or supplements, is the most potent stimulus of muscle protein synthesis. Consuming nonessential amino acids, either alone or with EAAs, has no impact.

EAA supplements have been shown to trigger muscle protein synthesis and increase muscle mass, strength, and physical function in at least 25 clinical trials. The muscle-building response to EAAs is 2 to 4 times greater than the muscle-building response to the same amount of a whey protein supplement. The muscle-building response to EAAs is even greater than the response to hormonal treatment with testosterone, growth hormone, or insulin.

There is one very big must when it comes to EAA supplementation, however. In order to be effective, all the EAAs are required. That being said, there are varying degrees of importance among the EAAs.

Leucine, which is both an EAA and a BCAA, is particularly important. Leucine is the most abundant EAA in muscle protein, so it should comprise the highest proportion of an EAA supplement. Beyond its role as a component of muscle protein, leucine can signal the molecular mechanisms within the cell to initiate the process of protein synthesis. Important as leucine may be, however, it cannot function alone. All the other EAAs are required as well, roughly in proportion to their relative content in muscle. It is not possible to make muscle protein from leucine alone.

The Role of Essential Amino Acids for Bodybuilding

It is clear from the above discussion that making sure you consume enough essential amino acids is an important part of bodybuilding. Even when using EAA supplements, the main source for your essential amino acids intake will likely be dietary protein. Therefore, the place to start is with your diet.

Protein is the key dietary component of the basic bodybuilding diet. It will increase your muscle mass. You should set a goal of eating approximately 30% of your caloric intake as high-quality protein.

When I say high-quality protein, I mean a protein that contains a high abundance of essential amino acids. High-quality proteins are generally animal-based proteins. These protein food sources also have a significant amount of non-protein calories. Therefore, eating a sufficient amount of high-quality protein to supply all the EAAs you need is difficult through normal diet alone.

You will most likely run into issues with the flexibility of your diet when eating this amount of high-quality protein food sources because of the non-protein calories. Therefore, EAA supplements can play a vital role in helping you meet your dietary goal for EAA intake.

While the focus of your basic diet should be high-quality protein, you must remember that energy substrates (carbohydrates and fat) are important too. As an example, in a tightly controlled study, subjects drank the same amount of protein in the form of milk. In one case, it was skim milk, and in the other case whole milk. The stimulation of muscle protein synthesis was greater with the whole milk. Under these study conditions, the additional calories provided by the fat in the whole milk helped to fuel muscle building.

You must be in a positive energy balance to gain a significant amount of muscle mass. Carbohydrate is of less importance for resistance training than it is for endurance training, but you should eat enough fruit and vegetables to meet the RDAs for micronutrients. Also, carbohydrate intake will stimulate insulin release, and insulin is an anabolic hormone that will increase the amount of muscle protein made from your EAA intake.

Fat intake will also amplify the anabolic effect of EAAs, and therefore you can eat animal-based, high-quality protein foods without worrying about eating too much fat.

What you do want to keep in mind with your bodybuilding diet is that the more you eat, the bigger you will get. If you do eat a lot while lifting heavy weights and consuming EAA supplements as recommended, a significant part of the weight gain will be muscle.

You will also gain fat with this dietary approach, so you need to carefully monitor your body composition to be sure that the extra fat you put on does not counteract the benefits of the muscle gain. In a sport like powerlifting, that is not likely to be the case, but if you are bodybuilding for appearance, you must reach a balance between muscle and fat gains. This can be accomplished by incorporating aerobic exercise into your training program.

How to Use Essential Amino Acids for Optimal Bodybuilding Results

amino acids for bodybuilding

The research documenting the optimal use of amino acids for bodybuilding is extensive. Experts can provide precise guidance on the effects of taking EAAs both pre-workout and post-workout.

Consuming 15 grams of EAAs 30 minutes before starting your workout will elevate blood concentrations of essential amino acids throughout your workout and stop the muscle breakdown that would otherwise occur. A 15-gram dose of EAAs achieves a greater response on muscle protein synthesis than either casein or whey protein can, without creating the fullness that can hinder a workout.

Then immediately after your workout, take another 15 grams of EAAs. One hour later, take another 15-gram dose.

These recommendations stem from the assumption that you will be working out every day. When you do take off days, you should still consume the same amount of EAAs. Instead of using your workouts to determine the timing, however, take your EAAs between meals.

Between the completion of dinner and breakfast the next morning, you may go for 12 hours or more without food. During this post-absorptive time, muscle tissue breakdown transpires in order to supply amino acids to tissues and organs that have no protein reserve. Therefore, to fuel maximal muscle-building response around the clock, you should consume another 15 grams of EAAs before bedtime. If you have wholly committed to maximizing muscle gain, you can even set your alarm for a final dose at about 4 am.

Alternatively, you can take 20 grams of casein protein at bedtime. Because casein coagulates in the stomach, your body digests it at a slower rate, meaning the amino acids it contains are then absorbed over many hours. While the anabolic effect will be less than if you take the EAAs, this approach will save you the trouble of getting up in the middle of the night.

The total amount of supplemental EAAs you ingest should be in the range of 60 grams per day. Consuming this amount of EAAs will stimulate the production of new muscle protein without you having to also take in a significant amount of non-protein calories. The result will be a lean body with increased muscle mass and minimal increase in fat mass. Sixty grams of EAAs in addition to what you eat as part of your bodybuilding diet is needed to drive protein synthesis past what may be your normal genetic limit.

Do EAA Supplements Have Side Effects?

This a reasonable question, because bodybuilding requires a much higher than average EAA intake. An important caveat to state up front is that I am focusing exclusively on side effects from EAA supplements.

When your EAAs come from an unusually high amount of dietary protein intake, that will increase the rate of amino acid oxidation and as a result, burden the kidneys to excrete the ammonia and urea that are natural byproducts of NEAA oxidation.

The great thing about EAA supplements, however, is that there is no such increased oxidation of NEAAs when EAAs are consumed. This is because NEAAs are not also being consumed but are rather being produced in the body. In fact, the oxidation of the NEAAs actually goes down, since they are being incorporated into protein at an increased rate.

Consequently, there is no reason to worry about the side effects of EAA supplements. The FDA has determined EAA supplements to be Generally Regarded as Safe (GRAS), while the Food and Nutrition Board of the National Academy of Science has determined that there is no upper limit of consumption beyond which would not be safe.

Leucine Muscle Building and Performance: The Magic Bullet?

Leucine has received special attention for its role in muscle building, not only because it is the most abundant EAA in muscle protein, but also because of its nutraceutical role as a regulator of muscle protein synthesis. Is leucine the “magic bullet” of muscle building?

Leucine is one of the nine essential amino acids (EAAs). EAAs are considered “essential” because the body can’t make them, and they must be consumed as part of the diet. Among the EAAs, leucine has received special attention for its role in muscle building, not only because it’s the most abundant EAA in muscle protein, but also because of its nutraceutical role as a regulator of muscle protein synthesis—the process of muscle building. But are these leucine muscle building benefits the “magic bullet,” or is leucine no more or less important than any of the other EAAs? The truth is that it falls somewhere in between.

What Is Leucine?

Leucine is one of the three branched-chain amino acids (BCAAs), the other two being isoleucine and valine. The term branched-chain refers to the chemical structure of these EAAs, which consists of branched side chains—the shorter chains of atoms attached to the main chain, or backbone, of the molecule.

Leucine is the best known of the BCAAs and is, as already mentioned, the most abundant EAA in muscle tissue. In addition, leucine acts as a signal to activate various cellular functions, including the process of protein synthesis.

How Muscle Protein Synthesis Works

Muscle protein is in a constant state of turnover, being continuously broken down and resynthesized. Muscle building takes place when the rate of muscle protein synthesis exceeds the rate of muscle protein breakdown. This can occur when there’s a stimulated rate of muscle protein synthesis, a suppression of muscle protein breakdown, or a combination of the two.

The process of muscle protein synthesis itself involves the hooking together of a series of amino acids in a very specific sequence and amount. Under normal conditions, most of the amino acids that hook together to form new muscle protein are those released during protein breakdown.

However, about 15% to 20% of the amino acids released during protein breakdown are not available to build new muscle protein. Some are irreversibly oxidized, while others are released into the bloodstream and taken up by other tissues and organs. For this reason, an additional source of amino acids is needed so that the rate of protein synthesis can catch up with, or exceed, the rate of protein breakdown.

Eleven of the amino acids in body protein are nonessential, which means the body produces them on its own to meet the demands of protein synthesis rates. By contrast, EAAs such as leucine must be consumed in the diet since they can’t be produced in the body. For this reason, consuming sufficient EAAs is mandatory for increasing the rate of muscle protein synthesis.

Leucine Muscle Building Supplements

Muscle protein can’t be built with leucine alone. In fact, for new muscle protein to be produced, all of the EAAs must be available in proportion to their respective contributions to the composition of that protein.

Since leucine is the most abundant EAA in muscle protein, comprising about 23% of the total EAAs, high leucine intake is essential for the production of muscle protein. Consequently, the profile of EAAs consumed for the purpose of stimulating muscle protein synthesis—whether in a natural protein food source or an amino acid supplement—must contain a relatively high proportion of leucine.

There’s no debate about the importance of leucine as a building block of muscle protein. Neither is there any controversy regarding the need for leucine to make up at least 20% to 25% of consumed EAAs to maximally stimulate muscle protein synthesis.

The question is, rather, whether the effects of leucine are so unique that this one substance should constitute a disproportionately greater amount of a dietary amino acid supplement compared with the other EAAs. In other words, is leucine supplementation alone beneficial for building muscle?

Keep in mind that this question is relevant only to amino acid supplements, as there is no natural protein source made up of more than 23% leucine, and there is no natural protein source that contains only leucine. So, in order to answer this, we must first understand leucine’s role as a nutraceutical.

Leucine has been called a nutraceutical because it has the ability to stimulate muscle protein synthesis on its own and is more than just one of the components of muscle protein. In fact, leucine can actually initiate the process of protein synthesis by activating a group of intracellular compounds known collectively as initiation factors.

The key initiation factor activated by leucine is a protein called mammalian target of rapamycin (mTOR), which acts as a sensor within the cell. When leucine concentrations are low, mTOR receives the signal that there’s not enough dietary protein present to build new skeletal muscle protein and is deactivated. But when the concentration of leucine within the cell increases, mTOR is activated.

Activation of mTOR can increase the amount of muscle protein produced, provided there are enough of the other EAAs (in addition to leucine) available to make complete proteins.

Muscle Protein Synthesis and mTOR

In normal, healthy adults, mTOR can be activated and muscle protein synthesis stimulated with a balanced EAA supplement, so there’s no need for extra leucine. However, in many clinical states, muscle protein synthesis is just not as responsive when EAAs are consumed, either as food or as supplements.

When this happens, it’s referred to as anabolic resistance—the reduced stimulation of muscle protein synthesis in response to protein intake. Anabolic resistance often occurs alongside conditions such as cancer or severe trauma or illness or during the regular process of aging.

During a state of anabolic resistance, an EAA supplement containing a disproportionately high amount of leucine (35% to 40%) may be needed to activate mTOR and overcome the resistance.

My team and I actually discovered this in 2006, when we studied the beneficial effects of an EAA mixture with leucine on muscle protein metabolism in elderly and young individuals. You can read about the study, published in the American Journal of Physiology, Endocrinology, and Metabolism, here.

But leucine is not the only way to activate mTOR. Resistance exercise can also further elevate mTOR, providing the potential for increased muscle protein synthesis. However, when engaged in resistance training, sufficient EAAs must be available for the further activation of mTOR to translate into increased protein synthesis.

Put simply, you can’t make something out of nothing. And that’s because a shortage of even one EAA will limit the stimulation of muscle protein synthesis, even after a heavy resistance workout. So while mTOR activation isn’t always linked to increased protein synthesis, it is an anabolic signal when all the necessary components are present.

Leucine Alone Isn’t Enough

The best way to envision the role of leucine in protein synthesis is to think of the EAAs as a football team, where leucine is the quarterback and the other positions are filled with other EAAs, each with their own specific role. Just as a team of only quarterbacks wouldn’t have much success in a game, a nutritional supplement wouldn’t have much success if it contained only leucine.

There have been a number of studies examining the effectiveness of leucine as a nutritional supplement. And as predicted by the analogy above, leucine alone has been shown to have little effect on muscle building—according to a 2011 study published in the Journal of Nutrition.

Compare these findings with a study we published in the journal Clinical Nutrition that showed how a formulation of EAAs with a high proportion of leucine (35% to 40%) helped overcome anabolic resistance and improve muscle mass, strength, and physical function in the elderly.

Leucine is important, but it can’t do the job alone!

Leucine and Muscle Protein Breakdown

The role of leucine in stimulating muscle protein synthesis has been studied extensively, but the building of muscle is determined not only by the rate of protein synthesis but also by the balance between the rates of synthesis and breakdown.

With this in mind, it’s interesting to note that leucine also has the ability to reduce the rate of muscle protein breakdown and, thus, muscle loss. One reason for this is that leucine can stimulate the release of the hormone insulin, and the suppression of muscle protein breakdown by insulin is well known.

As one of the BCAAs, leucine can also suppress protein breakdown directly. However, suppressing muscle protein breakdown only helps build new muscle if the rate of muscle protein synthesis is greater than the rate of breakdown, and this may not occur when consuming just leucine or BCAAs.

In fact, a reduction in muscle protein breakdown caused by leucine or BCAAs alone is accompanied by a corresponding reduction in the rate of muscle protein synthesis. This reflects the fact that the major source of EAAs for building new muscle protein is the EAAs that are released by protein breakdown. Therefore, if muscle protein breakdown is suppressed, the availability of EAAs for protein synthesis is also reduced.

As in the case of muscle protein synthesis, leucine can play a potentially important role in building muscle by inhibiting the rate of muscle protein breakdown, but to increase the anabolic response—meaning synthesis is greater than breakdown—all the EAAs must be consumed.

Leucine and Performance

Leucine is oxidized at an increased rate during endurance sports. This is evidenced in a study published in the Journal of Applied Physiology: Respiratory, Environmental and Exercise Physiology. Although a large portion of total energy production isn’t derived from leucine oxidation during exercise, the amount of leucine oxidized is significant in terms of the amount available for incorporation into protein.

In other words, the increased oxidation of leucine during exercise can make its availability—or lack thereof—limiting for the production of new muscle protein.

This is why it’s necessary to consume EAAs in general, and leucine in particular, post exercise. Consuming protein shakes, whey protein, or EAAs after exercise will not only prevent the loss in muscle protein that would occur otherwise (because of the oxidation of leucine) but will also increase muscle protein synthesis and increase muscle strength and function.

Leucine and Type 2 Diabetes

We’ve known for 50 years that blood concentrations of leucine (and the other BCAAs) are elevated in individuals with type 2 diabetes. This knowledge has spurred theories that the BCAAs, and leucine in particular, are somehow involved in the development of insulin resistance and, ultimately, type 2 diabetes.

A recently proposed theory that’s been gaining popularity is based on the premise that the activation of mTOR may be involved in causing insulin resistance. However, this theory is contradicted by studies that have shown that increasing leucine concentrations in dietary supplements not only doesn’t cause insulin resistance but may also, in some circumstances, actually improve blood sugar control.

Studies have also shown that supplementing with all the BCAAs can improve insulin sensitivity in a variety of insulin-resistant states.

Additional Benefits of Leucine

Leucine serves other functions as well. For example, it:

  • Increases the number of muscle mitochondria—the organelles where adenosine triphosphate (ATP) is generated to fuel muscle contraction during exercise
  • Promotes the growth and repair of bone tissue
  • Stimulates growth hormone production
  • Speeds wound healing

Perhaps the most important takeaway here is that leucine—like most things in life—can’t do what it does alone. It needs the help of all the EAAs to be the magic bullet of muscle building the body needs.

Is leucine the “magic bullet” of muscle building?

Tendonitis: When Tennis Elbow Has You Down for the Game

A painful condition, tendonitis involves inflammation of the tendons—fibrous cords connecting muscles to bones. Commonly occurring in the knees, heels, shoulders, elbows, and wrists, tendonitis leads to swelling and discomfort when moving the affected body part.

A painful condition, tendonitis involves inflammation of the tendons—fibrous cords that connect muscles to bones. Commonly occurring in the knees, heels, shoulders, elbows, and wrists, tendonitis leads to swelling and discomfort when moving the affected body part.

You might know tendonitis by the following terms:

  • Jumper’s knee (patellar tendonitis)
  • Tennis elbow (lateral epicondylitis)
  • Golfer’s elbow (medial epicondylitis)
  • Pitcher’s shoulder or swimmer’s shoulder (rotator cuff tendonitis)

Tendonitis is also spelled tendinitis, so don’t let those variations confuse you. Whatever you call it, tendonitis causes pain and discomfort that can have a negative effect on quality of life. And while the condition usually improves on its own with rest, more severe cases may require physical therapy, medication, and even surgery to heal. Understanding the signs and symptoms of tendonitis is the first step in knowing when and if to seek medical attention.

Common Causes of Tendonitis

The most common causes of tendonitis are sudden injury and repetitive motions, such as from physical activities that put stress on the tendons. If proper technique isn’t followed, tendonitis or tendon rupture can occur.

Risk factors for tendonitis include age— it’s inevitable that as we age, our tendons become less pliable—occupation, and certain sports. Jobs that involve repetitive movements or forceful action, such as frequent overhead reaching, can cause irritation of a tendon. Sports injuries that cause tendinitis are common among tennis players, runners, golfers, swimmers, bowlers, baseball players, and basketball players.

Tennis Elbow and Tendonitis Symptoms

Wondering if you’re suffering from tennis elbow or just a mild cause of overexertion? Here are some of the primary signs and symptoms of tendinitis:

  • Pain that worsens with movement
  • A cracking or grating feeling around the bone
  • Swelling
  • A lump near the affected tendon

Despite the name, tennis elbow often occurs in people who have never picked up a racket. In fact, the condition may occur in anyone whose work or hobbies involve repetitive motions of the wrist and arm. To that end, tennis elbow is common in painters, plumbers, and carpenters as well. Older people are more likely to get tennis elbow, as tendons become less flexible with age.

If you’re suffering from persistent pain around your elbow that spreads into the forearm and wrist, or if you’ve noticed a bony bump on the outside of your elbow, don’t hesitate to seek medical attention. Left untreated, tendonitis can cause a more serious condition called tendon rupture, which often requires surgery to repair.

Tendonitis Diagnosis

Your health care provider will determine if you have tendonitis or a related condition by taking a medical history and conducting a physical examination that assesses range of motion and discomfort in the affected area. Be upfront with your work and physical activities, including any new sports you’re trying out, so the doctor can consider contributing risk factors.

Your physician may also order X-rays to rule out arthritis or a fracture and blood tests to rule out conditions such as rheumatoid arthritis. Your doctor may even go a step further and order an MRI scan (magnetic resonance imaging) to see changes in the tissue around the tendon.

The type of test used is greatly determined by the area affected. For instance, the Finkelstein test helps diagnose wrist tendonitis. Your doctor will bend your thumb, fingers, and wrist in a specific manner to see if the pain that results is tied to wrist tendonitis or another type of wrist injury.

Tendonitis Treatments

There’s no one cure for tendonitis. The goal of treatment is to reduce pain and inflammation while giving the body time to heal. Some of the most effective home remedies for the condition include:

  • Resting and avoiding activities that led to the injury
  • Applying an ice pack to the affected area for 20 minutes every couple hours
  • Using a compress or bandage on the affected area
  • Elevating the limb or injured body part
  • Taking over-the-counter medication, such as ibuprofen

It’s important to note that tendonitis can take 4 to 6 weeks to heal. However, more serious or long-lasting cases of tendonitis may require additional treatment. If rest and medication are doing little to alleviate your discomfort, you might want to see a doctor and/or physical therapist to discuss the following treatment options:

  • Steroid injections to reduce inflammation and pain
  • Shockwave therapy
  • Platelet rich plasma injections to encourage healing
  • Surgery to repair tendon ruptures and remove damaged tissue

Note that it could take 6 months for a tendon to heal completely after surgery.

A painful condition, tendonitis involves inflammation of the tendons

Achilles Tendonitis Treatment

Athletes and other people who spend a lot of time on their feet are at risk for a type of tendonitis affecting the Achilles tendon. With Achilles tendonitis, the large tendon that runs down the back of the leg becomes inflamed. As a result, patients may suffer stiffness, swelling, and pain that worsens with activity. Treatments for Achilles tendonitis vary based on the severity of the condition and may include:

  • Rest and avoiding repetitive motions
  • Stretching and muscle-strengthening exercises
  • Icing the area
  • Elevating the affected foot
  • Physical therapy
  • Taking anti-inflammatories
  • Wearing special shoes to take tension off the tendon

In severe cases, patients may require steroid injections or surgery to treat their Achilles tendonitis.

What Is the Difference Between Tendonitis and Tendinosis?

Tendonitis involves inflammation. When tendonitis is at play, you’ll see hallmark inflammatory signs such as warmth, swelling, redness, and pain. Take wrist tendonitis, for example. Wrist tendonitis involves inflammation of the wrist tendons and is caused by either a sudden injury or repetitive motions that cause the wrist tendons to rub against the bone. Over-the-counter nonsteroidal anti-inflammatory drugs (NSAIDS) such as ibuprofen can help the pain as the tendonitis subsides over the course of several weeks.

Tendinosis, on the other hand, is chronic, which means continuous or recurring. It’s caused by a repetitive trauma or overuse injuries, and can take several months to heal. The main difference between tendonitis and tendinosis is that tendinosis is the the non-inflammatory degeneration of a tendon.

Amino Acids as a Tendonitis Cure

An increasing amount of research suggests that amino acids can boost musculoskeletal health and even help repair damage. When people engage in exercise, their muscles break down more rapidly, and additional protein is required to prevent minor injuries from becoming serious ones.

According to a 2018 article titled “Nutritional Research May Be Useful in Treating Tendon Injuries,” evidence suggests that certain amino acids, including leucine, arginine, and glutamine, can aid in tendon growth and healing. However, it’s always best to consume a balanced mixture of essential amino acids to ensure optimal health and wellness.

The article goes on to reveal that tendon surgery isn’t always successful, and many patients experience chronic pain even after treatment. More research is needed to determine if amino acids could be used in therapeutic approaches to tendon injuries and other problems.

Additionally, people can protect their long-term tendon health by avoiding exercises and activities that put undue stress on tendons. It’s also smart to mix up workout routines, take time to stretch and warm up, and use ergonomic equipment in the workplace.

The Relationship Between Energy and Amino Acids

Energy is one of the primary markers of health. When people are asked about their health, low energy is often a common complaint. What many people don’t realize, however, is that energy and amino acids go hand in hand.

Energy is one of the primary markers of health. When people are asked about their health, low energy is often a common complaint. Likewise, when people are asked to identify a benefit from a nutritional supplement, “improved energy” is often the first thing they report. What many people don’t realize, however, is that energy and amino acids go hand in hand.

Almost everyone, even the most energetic among us, desires more energy. So it’s no accident that energy drinks have become so popular. However, the concept of energy is somewhat vague. What does having energy really mean?

To understand the relationship between energy and amino acids, we must first distinguish between physical and mental energy. These two types of energy are clearly related, but distinct. By considering physical and mental energy separately, we can better understand the physiologic basis for each.

Energy and Amino Acids: What Fuels Our Bodies?

Physical energy requires not just fuel for our bodies but also all the necessary vitamins and cofactors—the inorganic substances needed for certain enzymes to carry out their functions—required to convert food to an energy form our cells can utilize.

Assuming all vitamins and cofactors are available, the energy necessary for physiologic functions is derived from combining carbohydrates, fats, proteins, and (in some cases) alcohol with oxygen in a process known as oxidation. These energy substrates—molecules acted on by an enzyme—can thus be considered the “fuel” of the body.

The major form of chemical energy in the body is a compound called adenosine triphosphate (ATP). Energy is released when ATP is broken down to adenosine diphosphate (ADP) and phosphate.

ATP is regenerated by the metabolism of the macronutrient (food required in large amounts for optimum nutrition) energy substrates mentioned above as well as by the oxidation of amino acids.

Chemical Energy and Mitochondria

The energy needed to perform physical functions such as exercise comes from the chemical energy stored in ATP. ATP is the universal fuel used by all cells.

In general, food is digested and absorbed as its basic components (glucose and other simple sugars, fatty acids, and amino acids), which are then used for structural needs, stored away, or oxidized for energy.

The oxidation of nutrients into chemical energy involves complex biochemical pathways. The Krebs cycle, named for its discoverer, Sir Hans Adolf Krebs—and also known as the citric acid or tricarboxylic acid (TCA) cycle—involves a series of chemical reactions in which carbon structures derived from carbohydrates, fats, and proteins are metabolized, with the production of ATP as a byproduct.

The TCA cycle operates inside mitochondria, which are specialized organelles within cells that are responsible for “digesting” nutrients and turning them into energy.

The energy and amino acid relationship.

Oxidation of Amino Acids for ATP Production

The majority of physical energy comes from the oxidation of fats and carbohydrates. However, every amino acid in the body can potentially be oxidized to produce ATP.

The amount of oxidation undergone by the essential amino acids (or EAAs)—the nine dietary amino acids that can’t be produced in the body and must be obtained from food—determines how much of each essential amino acid you need in a day.

The amount of protein synthesized by the body will decrease if a steady supply of EAAs is not maintained, leading to conditions such as muscle loss and impaired immune function. Therefore, any EAA that is oxidized must be replaced through the diet.

The oxidation of EAAs is important physiologically even though only a minimal amount of total energy production is derived from this process. For example, at rest, less than 10% of energy production comes from the oxidation of amino acids.

Exercise greatly increases the requirements for ATP, and part of that ATP comes from amino acid oxidation. This is one reason why the consumption of a number of whole foods and supplements, including whey protein, is recommended in the field of sports nutrition both pre-workout and post. However, amino acid oxidation does not increase uniformly during exercise.

Among the EAAs, there is a selective increase in the oxidation of leucine. However, even with the increase seen during exercise, leucine oxidation provides only about 3% to 4% of energy for ATP production. Yet leucine plays a crucial role in regulating protein synthesis and other metabolic processes, so extra leucine needs to be consumed after exercise to replace what was oxidized.

While amino acids, particularly EAAs, do not play a major role in overall energy production, there are a number of aspects of amino acid oxidation that are important for the body’s metabolic regulation. To understand the critical nature of EAA oxidation is to appreciate that the body regulates the availability of all EAAs at a relatively constant level.

Consuming a high-protein meal causes EAA availability to increase. This increased concentration of EAAs stimulates their oxidation and minimizes changes in EAA availability. By contrast, if you do not consume enough EAAs through your diet, metabolic adaptations occur that reduce the rate of EAA oxidation.

The oxidation of specific amino acids is important for the body. For example, the availability of certain amino acids depends on the oxidation of other amino acids.

Take tyrosine, for example. This amino acid is produced in the liver from the oxidation of the EAA phenylalanine. Maintaining an adequate amount of tyrosine in the blood is critical, as tyrosine is a precursor of the neurotransmitters dopamine, norepinephrine, and epinephrine.

Specific tissues and organs also have metabolic preferences for certain amino acids. Most prominently, glutamine (a nonessential amino acid) is a preferred substrate for the gut.

Amino Acids Augment Mitochondria

Only recently have we begun to appreciate the difference in energy levels the number of available mitochondria and their ability to operate at full capacity can make. Both amino acid supplementation and exercise are known to increase numbers of mitochondria and enhance their function.

By contrast, alcohol or drug use has been shown to induce mitochondrial defects by increasing oxidative stress and damaging mitochondrial genetic material—deoxynucleic acid, or DNA. When alcohol damages mitochondrial DNA, it impairs mitochondrial function, which further increases oxidative cell stress, leading to a vicious cycle of accumulating cell damage and decreased energy production over time.

Mental Energy: What Balances Our Brains?

Energy drinks typically contain caffeine (with a range of 6 to 242 mg of caffeine, according to Consumer Reports) and perhaps some B vitamins.

Whether used to help one wake up first thing in the morning or as an afternoon pick-me-up, these beverages clearly aid in sharpening concentration and increasing the body’s overall feeling of energy.

Surprisingly, when it comes to maintaining mental energy and focus, amino acids play as important a role as caffeine. In contrast to caffeine, however, amino acids impact mental energy by modulating neurotransmitters within the brain.

Many of the brain’s neurotransmitters are produced through the conversion of amino acids as they pass through the blood-brain barrier. In addition, two amino acids—glutamate and aspartate—are themselves considered neurotransmitters.

The interaction of neurotransmitters in the brain determines many aspects of behavior. To simplify a very complex system, the key determinant of mental energy is the balance between the neurotransmitters dopamine (excitatory) and serotonin (inhibitory).

The amounts of dopamine and serotonin in the brain are dependent on the availability of the precursors for their productionTyrosine is the amino acid precursor of dopamine, and tryptophan is the amino acid precursor of serotonin.

Tyrosine is also derived from the oxidation of phenylalanine. However, neither phenylalanine nor tryptophan is made in the body, as both are EAAs.

Increasing the amount of phenylalanine consumed in the diet will, via conversion to tyrosine, increase mental energy by increasing the amount of dopamine in the brain.

Conversely, increasing tryptophan consumption, such as through the use of the dietary supplement L-tryptophan, will induce a feeling of sleepiness or lack of energy by promoting serotonin production.

Amino Acid Balance and Mental and Physical Energy

Amino acids help support both physical and mental energy via a wide range of actions. While supplementation with individual amino acids may produce particular reactions, disrupting the body’s balance by consuming a single or small combination of amino acids may be counterproductive when it comes to other functions.

An amino acid supplement containing relatively high levels of phenylalanine (tyrosine is nearly insoluble and difficult to add to a dietary supplement) and low levels of tryptophan can provide mental sharpness and focus. However, an isolated increase in phenylalanine can also induce Parkinson-like symptoms in susceptible individuals.

Likewise, consumption of leucine can counter the accelerated rate of oxidation that occurs during exercise, but the use of leucine in isolation will activate the oxidation of valine and isoleucine, thereby limiting muscle protein synthesis.

Consequently, to replace the oxidized leucine and enhance post-workout muscle recovery, it is necessary to provide all three of the branched-chain amino acids, or BCAAs—leucine, isoleucine, and valine.

Finally, all EAAs must be available in sufficient quantities to stimulate muscle protein synthesis, which is the metabolic basis for increased muscle growth, strength, and function.

Hence, the gold standard approach for the maintenance of both mental and physical energy involves choosing a free-form amino acid formulation that takes into account not only the direct actions of the component amino acids but also the importance of maintaining a relative balance of EAAs to sustain maximal benefit.

BCAAs and EAAs—Which Amino Acid Supplement Is Right for You?

If you search for “essential amino acids” on Google you will see many sites advertising branched-chain amino acids (BCAAs), and others advertising essential amino acids (EAAs). You may be left wondering: Are BCAAs and EAAs the same thing? If not, what’s the difference? Which is right for you?

Discussions of amino acids are rife with acronyms, but the two most common just might be BCAAs and EAAs.

If you search for “essential amino acids” on Google, the top results will be filled with sites proclaiming the health benefits of branched-chain amino acids, or BCAAs. And you’ll also discover just as many sites where prominent experts in sports nutrition claim that BCAAs are worthless and the true heroes of the amino acid world are essential amino acids, or EAAs.

Understandably, you may be left wondering about the differences between BCAA supplements and EAA supplements. With all the strident advertising claims, it can be quite challenging to determine the basic facts about both types of amino acids, let alone which supplement option will be right for you.

Essential Amino Acids (EAAs) Explained

Essential amino acids (EAAs) belong to a broader class of amino acids involved in protein synthesis and fittingly referred to as proteinogenic amino acids. One of the primary ways your body uses these amino acids, which have been nicknamed the building blocks of protein, is for muscle growth.

The class of proteinogenic amino acids can be split into two primary subcategories: essential amino acids (EAAs) and nonessential amino acids. Nine amino acids have been classified as essential because the human body cannot synthesize these on its own, meaning you must obtain them from dietary protein sources or nutritional supplements. The nine essential amino acids are:

Leucine Lysine Tryptophan
Isoleucine Threonine Histidine
Valine Phenylalanine Methionine

While the nonessential amino acids undeniably contribute to your overall health and well-being in crucial ways, the human body can produce them from a combination of essential amino acids, carbohydrates, and fats, rendering them comparatively nonessential.

EAAs play a variety of important roles in the body, including acting as precursors for the production of brain neurotransmitters and supporting immune function. However, as I mentioned above, the main role of EAAs is as constituents of proteins, including muscle protein.

Since all proteins in the body are continually broken down and re-synthesized, an adequate supply of all the EAAs is required or body protein will be lost. Most of the EAAs in body protein that is released as a result of protein breakdown are available for reincorporation into protein. However, approximately 15% of the EAAs released from protein breakdown are oxidized, which means they are irreversibly lost. The EAAs that are oxidized must be replaced through your diet since they cannot be produced in the body.

Branched-Chain Amino Acids (BCAAs) Explained

Branched-chain amino acids (BCAAs) exist as a subcategory of essential amino acids. The three branched-chain amino acids—leucine, isoleucine, and valine—got their name because of their distinctive, branch-like chemical structures.

When it comes to BCAA benefits, leucine dominates. Researchers have proposed that leucine holds a variety of regulatory roles in the body. Initial interest in the unique qualities of leucine concerned its primary role in stimulating muscle protein synthesis, or the building of new muscle tissue. We can trace this interest back to a 1975 study published in the Journal of Clinical Investigation that demonstrated leucine’s capacity to stimulate protein synthesis in isolated rat muscle.

Then in 1988, two scientists named Garlick and Grant conducted studies with rats to explore the possibility that the same effect could be elicited in a living creature. Their findings showed that a mixture of BCAAs could increase the muscle protein synthesis response to insulin.

The next major advance came in 2000 when the Journal of Nutrition published a study that investigated the potential mechanism by which leucine acts as a stimulator of muscle protein synthesis. The study authors showed that leucine ingestion stimulated muscle protein synthesis in rats and that the increase in synthesis was accompanied by the activation of several molecular factors (including the mTOR pathway) within the muscle cell that are required for initiation of the process of protein synthesis.

Researchers refer to these factors collectively as the initiation factors, and the entire molecular processes involved in the initiation of protein synthesis as anabolic signaling. The takeaway, at this point, was that leucine can activate anabolic signaling.

But an interesting phenomenon occurred when humans entered the research picture. When scientists began to study the beneficial effects of leucine on human subjects, it became evident that providing leucine alone disrupted the balance of plasma amino acids. Most notably, increased availability of leucine not only caused increased oxidation of leucine but the accelerated oxidation of the other two branched-chain amino acids as well.

Because providing leucine alone created isoleucine and valine deficiencies, supplement companies typically formulate their proprietary blends of BCAAS to contain all three amino acids even though no special qualities of either valine or isoleucine have been identified.

Based on both historic and recent studies, we now have a good grasp of what happens when humans take branched-chain amino acid supplements. Scientists have shown that taking between 2 and 4 grams of leucine as part of a complete BCAA dietary supplement may positively influence a variety of physiological endpoints, including increased muscle mass, improved recovery from exercise, and enhanced mood and cognitive performance during prolonged exercise.

There is no doubt that leucine can be considered a nutraceutical, a designation that honors its regulatory effects beyond its role as one of the building blocks of body proteins. It’s clear that increasing the amount of leucine you consume each day can help you to build muscle and optimize your exercise performance, among other benefits.

What You Should Know About Muscle Protein Synthesis

As I briefly noted in the section on EAAs, one of the major contributions amino acids make in the human body is the stimulation of muscle protein synthesis.

In fact, researchers have discovered that the availability of the essential amino acids determines the rate of muscle protein synthesis. That means that the smaller the number of available EAAs, the slower the rate of muscle protein synthesis, and the larger the number, the faster the rate.

Every time you eat a food that contains all nine essential amino acids, or take an EAA supplement, you stimulate muscle protein synthesis. The degree of stimulation of muscle protein synthesis by EAAs depends on the dose. The more EAAs ingested, (with a maximum threshold of 15 grams), the greater potential for building muscle. Conversely, if EAAs in the blood drop below a certain level, then your muscle-building potential becomes compromised. You can learn more about this process in my book, A Guide to Amino Acid and Protein Nutrition: Essential Amino Acids for Everyone.

The most important takeaway about the relationship between amino acids and muscle protein synthesis is that all the essential amino acids are required to make new protein. This can best be understood by thinking about how proteins are made.

Each protein in the body is a long string of amino acids linked together in a specific order. Protein is produced by hooking together amino acids one by one in the order dictated by messenger RNA in the cell. If a point is reached where the next amino acid due to be incorporated into the chain is not there, production of the protein will stop.

Where Do the Amino Acids for Protein Synthesis Come From?

The proteins that make up your muscles constantly break themselves down and then build themselves back up. The muscle breakdown process releases amino acids, which your body then recycles and uses for the synthesis of new proteins. In the basal state, the resting metabolic state of the body in the morning after 12 hours of fasting, amino acids released by muscle breakdown serve as the main source of amino acids for protein synthesis. Regardless of your metabolic state, approximately 85% of the amino acids released by muscle protein breakdown are re-used in the protein synthesis process.

There are two ways to increase the rate of protein synthesis: either you find a way to more efficiently reutilize the amino acids from protein breakdown, or you make more essential amino acids available by increasing your consumption of EAAs.

The bottom line? The simplest and most effective way to ensure that all the EAAs will be available for muscle protein synthesis in the optimal ratios is to increase your intake of essential amino acids.

BCAA or EAA Supplements—Which Are Better for Muscle Growth and Muscle Repair?

Now it’s time to get down to brass tacks and settle the question of EAAs vs. BCAAs. To do so, let’s review what we’ve discussed so far. All three branched-chain amino acids—leucine, valine, and isoleucine—are also essential amino acids. They’re also all components of muscle protein. Plus, leucine can increase the efficiency of protein synthesis by activating the initiation factors. So, does that mean increasing your intake of leucine with a BCAA supplement is the best way to achieve desirable health outcomes like the stimulation of the synthesis of new muscle protein?

Not quite. Remember, if only BCAAs are consumed, they are limited in their ability to stimulate muscle protein synthesis. That’s because all the EAAs are required for a complete protein to be produced, and in the basal state, the only source of EAAs is from protein breakdown. Since most of those EAAs are already reincorporated, the maximal increase in protein synthesis is limited by the availability of the other EAAs. For this reason, research has shown that taking BCAAs alone has either no effect or a minor effect on the rate of muscle protein synthesis in human subjects.

There is no question that BCAAs are important for many functions in the body, including protein synthesis. However, the full benefit of BCAAs cannot be achieved if they are taken by themselves, because you cannot make a complete protein out of just three amino acids. The maximal effectiveness of the BCAAs is only achieved when they are taken along with the other six EAAs. Only a mixture of all the EAAs can provide a sustained stimulation of muscle protein synthesis. The nonessential amino acids in protein can be made in the body and are therefore not required in a dietary supplement.

A non-scientific analogy might be helpful in understanding the difference between BCAAs and EAAs. Think of EAAs like different players on a football team. In this analogy, leucine is the quarterback that calls the signals and is the most important player on the team—what team wins without a good quarterback? However, a team of just quarterbacks wouldn’t be very successful, and neither is an amino acid supplement made up entirely of grams of leucine.

All the positions on the team have an essential role to play, and without enough players for each position, the team will fail. Similarly, all the EAAs are required for the effects of leucine to translate to increased production of muscle protein. Consumption of a dietary supplement containing a balanced mixture of all the EAAs that includes a generous proportion of leucine is necessary for maximal results.

Beta-Alanine and Carnosine: Which Supplement Should I Take?

Beta-alanine and carnosine have a relationship worth exploring. With all the marketing claims of beta-alanine and carnosine supplements, there’s some confusion. Let’s set the beta-alanine and carnosine record straight.

For supplement connoisseurs, beta-alanine and carnosine have a relationship worth exploring. Carnosine helps you reach peak performance during high-intensity exercise, and beta-alanine helps boost carnosine levels in muscle. With all the marketing claims of beta-alanine supplements and carnosine supplements, there’s quite a bit of confusion in between. Let’s set the beta-alanine and carnosine record straight.

Beta-Alanine and Carnosine’s Relationship

Beta-alanine (also known as b-alanine, β-alanine, and a carnosine precursor) is an amino acid produced in the liver. It differs structurally (but not chemically) from its more abundant counterpart L-alpha-alanine.

L-alpha-alanine is one of the most abundant nonessential amino acids in the body. L-alpha-alanine serves as a constituent of almost all proteins in the body and plays an important role in shuttling nitrogen—released as a byproduct of amino acid degradation in muscle—to the liver. The liver then incorporates some of the L-alpha-alanine into proteins, and the leftover L-alpha-alanine serves as a precursor for the production of urea, which is then excreted in urine.

In contrast to L-alpha-alanine, beta-alanine is not credited with serving any direct role in the body. Beta-alanine is neither a component of body protein nor does it play a role in metabolic regulation (the process by which our cells regulate every chemical process required for life). The principal role of beta-alanine is to combine with the amino acid histidine to form the peptide carnosine. Benefits of beta-alanine on exercise performance are attributed to its role in the production of carnosine in muscle.

What Science Tells Us About Carnosine

Found in abundance in meat, poultry, and fish, carnosine (sometimes referred to as L-carnosine) is a dipeptide composed of two amino acids, beta-alanine and L-histidine, hooked together. A non-enzymatic free radical scavenger and natural antioxidant, carnosine mainly hangs out in muscle and brain.

Carnosine acts to reduce the rate of formation of a variety of substances that can be factors in the development or exacerbation of diseases including diabetes, atherosclerosis, chronic renal failure, and Alzheimer’s disease.

Researchers have found that carnosine can be particularly helpful when it comes to preventing damage caused by excessively high levels of sugar in the body. Both glucose and fructose molecules can bind with proteins, a process known as glycosylation. Not only does this damage the protein molecules, but it also stimulates inflammatory processes throughout the body. In fact, the glycosylation of protein is one of the four major destructive pathways activated by oxidative stress.

The metabolic effects of carnosine have contributed to its reputation as an “anti-aging” nutrient. As with other anti-aging compounds, carnosine levels decline with age. However, your carnosine intake affects the levels of carnosine in your muscle cells and throughout your body more than any other factor, including your age.

Carnosine helps you reach peak performance during high-intensity exercise, and beta-alanine helps boost carnosine levels in muscle.

How Carnosine Impacts Exercise

We’ve known for more than 50 years that carnosine functions as a buffer against acid produced in muscles during high-intensity exercise. The importance of carnosine as a buffer is debated, but there is a consensus that increasing muscle carnosine concentrations improves exercise performance during high-intensity activities. It is important, however, to understand the relationship between acid/base balance and exercise in order to appreciate the limit of circumstances in which carnosine in both Type 1 and Type 2 muscle fibers extends its benefits.

When you engage in high-intensity exercise, hydrogen ions begin to accumulate in your muscle fibers. This leads to an increase in acid production and drop in intramuscular pH, which adversely impacts your performance.

Can you recall the burning sensation you feel in your muscles when you sprint? The feeling that tells you it will be impossible to sustain that level of exertion for longer than a few minutes? That’s the result of lactic acid accumulation.

If lactic acid were to build up in exercises of the non-high-intensity variety, such as endurance sports, there would be no endurance athletes, as a buildup of lactic acid cannot be sustained beyond a short period of time. A consequence of this effect is that even competitive endurance exercise is performed below the “lactic acid threshold,” or the level of exercise intensity that can be performed without any buildup of lactic acid. For example, lactic acid levels remain close to the minimal level throughout a marathon. The action of carnosine on buffering acid production in muscle can, therefore, only be expected to be of significant benefit during high-intensity exercise. This may be why the body innately produces higher concentrations of carnosine in the fast-twitch, Type 2 muscle fibers that power you through rapid, explosive movements.

Research indicates that boosting muscle carnosine synthesis can reduce the acidity in active muscles during high-intensity exercise. A Belgian research team examined how muscle carnosine content affects fatigue experienced by trained sprinters during repeated isokinetic contraction bouts. Their placebo-controlled, double-blind study found that increased levels of carnosine significantly decreased fatigue during repeated bouts of exhaustive dynamic contractions.

In addition to its buffering capacity, carnosine has several other physiological effects that can improve your athletic performance.

As I stated earlier, carnosine has impressive antioxidant properties. Levels of a type of free radical called reactive oxygen species (ROS) can spike during exercise, which some believe may increase muscle fatigue. Carnosine can help to flush those free radicals from your muscles, which may lower fatigue levels.

Carnosine also influences enzyme regulation related to activation of myosin ATPase your body uses to maintain ATP stores. As you may know, your body generates energy from its ATP (adenosine triphosphate) stores.

Research-Backed Benefits of Beta-Alanine

The primary focus of research conducted to date on beta-alanine supplementation has been the effect of beta-alanine on physical performance and body composition.

Carnosine helps you reach peak performance during high-intensity exercise, and beta-alanine helps boost carnosine levels in muscle.

The effect of beta-alanine supplementation on muscular endurance has the most research behind it. At least eight high-quality studies have shown that beta-alanine can lead to a significant increase in muscular endurance.

According to a double-blind trial published in Amino Acids, a peer-reviewed journal, after 28 days of beta-alanine supplementation, participants experienced less muscle fatigue and had a greater workload capacity at peak exhaustion.

The beneficial effects of beta-alanine supplementation on power output have also been well-documented. The authors of a study published in the International Journal of Sports Medicine had participants complete a resistance-training program while taking 4.8 grams of beta-alanine daily for 30 days. They found that this level of beta-alanine supplementation resulted in impressive gains as measured both by power output and work volume. One particularly indicative finding: at the end of the trial, participants who supplemented with beta-alanine could perform 22% more repetitions at 70% of their one-repetition maximum than those in the placebo group.

Beta-alanine can also influence your body composition by encouraging fat loss and stimulating muscle growth.

According to a double-blind, placebo-controlled study conducted by researchers from the Human Performance and Physical Education Department at Adams State College in Colorado, beta-alanine supplementation can lead to the loss of fat mass without accompanying decreases to muscle mass.

The authors of a separate double-blind trial looked at the results of combining beta-alanine supplementation with high-intensity exercise. Participants who supplemented with beta-alanine while engaged in 6 weeks of high-intensity interval training benefited from a number of improvements that the placebo group who carried out the same training regimen did not, including increased lean body mass.

Beta-alanine supplementation can also enhance your anaerobic capacity, which has major implications for endurance performance. When you run, swim, cycle, or carry out any other form of aerobic exercise at a fast speed for a long enough period of time, your body will reach a point at which it’s consuming the maximum amount of oxygen it can. This is the moment when your anaerobic capacity comes into play. The greater the capacity of your muscles to work anaerobically—without the addition of more oxygen—the faster and longer you’ll be able to sustain that pace.

Findings published in Medicine & Science in Sports & Exercise and elsewhere have shown that beta alanine supplementation can positively affect your anaerobic capacity. This effect appears to stem from improved muscular endurance and reduced fatigue rather than cardiopulmonary interactions.

A number of studies have found that beta-alanine can help you exert yourself at a higher rate for longer periods of time while preventing fatigue. One study published in Nutrition Research showed that beta-alanine supplementation can lead to measurable decreases in fatigue rates, particularly when participants were working at maximum capacity. Subjective feelings of soreness and fatigue were also lower for the participants taking beta-alanine supplements than for those in the placebo group.

A separate double-blind, placebo-controlled study specifically examined how beta-alanine affects neuromuscular fatigue. The study’s authors enrolled participants with an average age of approximately 73, since the aging process depletes skeletal muscle carnosine content, which has been linked to a reduced muscular buffering capacity that then results in increased rates of fatigue. The authors found that beta-alanine markedly delayed the onset of neuromuscular fatigue and led to significant increases—28.6%—to participants’ physical working capacity at the fatigue threshold.

The Pros and Cons of Carnosine Supplements

Carnosine supplements are available from a variety of sources and marketed as being able to slow the aging process and help prevent and treat complications of diabetes. Carnosine supplementation is also advocated as a treatment for cardiometabolic health and cognitive function.

Despite the multitude of beneficial effects credited to carnosine in the body, there are limitations to its value as a nutritional supplement. Orally ingested carnosine is rapidly broken down to its component amino acids (beta-alanine and histidine). Plus, scientists have repeatedly found evidence of poor intestinal absorption of carnosine. For example, one study found large amounts of carnosine—up to 14% of the ingested dose—in participants’ urine 5 hours after they had ingested it.

Furthermore, a diet of beef, pork, and chicken is rich in carnosine, and the amount of carnosine recommended for a dietary supplement (1 gram per day) adds an insignificant amount to the total daily intake for meat eaters. Therefore, carnosine supplementation is not an effective way to increase the amount of carnosine in muscle. In the case of a vegetarian diet, carnosine supplementation may play a more prominent role in maintaining carnosine concentration in muscle.

Why Most People Benefit More from Beta-Alanine Supplements

The production of carnosine in muscle is limited by the availability of beta-alanine. As a result, dietary supplementation with beta-alanine is advocated as the most effective way to increase carnosine levels in muscle. The International Society of Sports Nutrition has issued a position statement on the effectiveness of beta-alanine as a nutritional supplement to raise muscle carnosine levels. The highlights of this report are as follows:

  1. Four weeks of consuming 4-6 grams of beta-alanine daily significantly increases muscle carnosine levels.
  2. Beta-alanine supplements appear to be safe.
  3. Tingling is the only reported side effect.
  4. Daily supplementation with 4-6 grams of beta-alanine improves high-intensity exercise performance in events lasting 1-4 minutes.
  5. Daily supplementation with beta-alanine may reduce the impact of neuromuscular fatigue in older subjects.
  6. Combining beta-alanine supplements with other supplements (such as essential amino acids) may be beneficial.

Carnosine Supplementation vs. Beta Alanine Supplementation: The Bottom Line

Carnosine can act as a buffer in muscle, thereby lessening the effects of excess acidity resulting from high-intensity exercise. This effect can improve high-intensity exercise performance but is unlikely to have much effect on endurance exercise. Other beneficial effects have been proposed (although not proven). Carnosine supplementation is ineffective in increasing the amount of carnosine in muscle because it is broken down to its constituent amino acids before tissue uptake can occur.

Beta-alanine is not known to have any direct physiological role but is the rate-limiting factor for carnosine synthesis. Studies have shown that beta-alanine supplementation can increase muscle carnosine content, and therefore, the buffering capacity of your muscles. This can result in significant improvements to physical performance as well as body composition.

Carnosine helps you reach peak performance during high-intensity exercise, and beta-alanine helps boost carnosine levels in muscle.

If you’re seeking to benefit from increased concentrations of carnosine, supplementing with carnosine itself is not the best way to achieve that goal. Instead, you’ll see far more profound effects from beta-alanine supplementation.