Amino Acids and Kidney Disease

Amino acids and kidney disease are inextricably linked. There is no circumstance in which the judicious use of dietary essential amino acids can provide more unique benefit than kidney disease.

Amino acids and kidney disease are inextricably linked. The kidneys are responsible for excreting metabolic waste products, including urea and ammonia, which are the end products of amino acid metabolism. Kidney disease is characterized by the failure to effectively clear these and other compounds from the blood.

Many individuals have a degree of kidney disease. Approximately 60% of people over the age of 65 have some impairment in renal function. This gradual decline in kidney function is called chronic kidney disease (CKD) or chronic renal failure and affects over 30 million Americans. The biggest risk factors for developing renal disease are high blood pressure, cardiovascular disease, insulin resistance, and diabetes, all of which put excess stress on the narrow blood vessels in the kidneys.

Monitoring Kidney Health

Kidney health is typically measured by looking at the GFR (glomerular filtration rate), which is a measure of how well the kidneys are filtering toxins from the blood. As part of a blood test a doctor will measure the kidneys’ ability to handle the waste product creatinine in what is called the creatinine clearance rate, and from this, the doctor can measure the rate at which blood is being filtered through the kidneys. The National Kidney Foundation recommends that GFR tests be performed regularly as part of an annual physical exam since early detection can help stop the progression of the disease.

Kidney Failure and Muscle Loss

In addition to causing massive oxidative stress that can result in a cardiovascular event such as a heart attack, kidney failure induces the stress response, and by association, loss of muscle mass and strength. The onset of the stress response is brought about in part by inflammation, as well as hormonal responses, including elevations in cortisol and epinephrine. In addition, the accumulation of urea and ammonia acidifies the blood, which has a direct inhibitory effect on muscle protein synthesis and can cause metabolic acidosis. The result is a profound loss of muscle mass and strength that has many unfavorable consequences.

Kidney Failure and Protein Intake

When kidney function is adequate, excreting the urea and ammonia produced from the metabolism of dietary protein intake is not an issue. In fact, it is well established that high-protein intake does not cause kidney failure when kidney function is normal. Unfortunately, with kidney failure, dietary protein has to be limited because of the impaired secretion of urea and ammonia.

Anabolic resistance—the compromised ability of the body to build muscle protein—is difficult to overcome in any circumstance but is particularly problematic when it comes to kidney disease. It would seem logical that the most effective dietary approach to anabolic resistance would be to consume a high-protein diet because protein metabolism fuels muscle protein synthesis. However, consumption of large amounts of dietary protein increases urea and ammonia production due to the metabolism of the absorbed amino acids that are not incorporated into protein. This is a high metabolic price to pay since anabolic resistance minimizes the effectiveness of protein intake.

Consequently, a low-protein diet is usually recommended for chronic kidney disease patients. While a protein-restriction diet minimizes the amount of urea and ammonia in the blood, in the setting of anabolic resistance a low-protein diet accelerates the rate of muscle loss. Because the importance of maintaining muscle mass is becoming much more widely appreciated, many experts in kidney disease are torn between the traditional recommendation for CKD patients to eat a low-protein diet and the adverse effects a low-protein diet has on muscle mass and function.

Essential Amino Acids and the Kidney

There is no circumstance in which the judicious use of dietary essential amino acids can provide more unique benefit than kidney disease. A brief overview of the relationship between amino acids and the kidney should make clear the role of dietary essential amino acids in lessening the devastating loss of muscle mass and function that normally occurs with kidney disease.

Muscle protein is in a constant state of turnover—protein is being broken down and releasing the component amino acids into the cell (protein breakdown), while at the same time cellular amino acids are being incorporated into new protein (protein synthesis). Part of the process of muscle protein turnover also involves the release of amino acids into the blood. While some of those amino acids released by muscle are taken up by other tissues and organs and incorporated into protein, others travel to the liver for metabolism, resulting in the production of urea and ammonia. The balance between protein synthesis and breakdown is determined by the rate of these various processes that are all occurring simultaneously.

The free amino acids in muscle cells are derived from blood, protein breakdown, or, in the case of the nonessential amino acids, production from other amino acids. In turn, cellular amino acids may be incorporated into protein or released into the blood in their original form. Additionally, they may be partially metabolized, and the nitrogen transferred to form the nonessential amino acids glutamine and alanine.

Glutamine and alanine are the major vehicles that transport nitrogen from muscle to the liver, where the nitrogen is then converted to urea and ammonia and released into the blood. The blood is filtered by the kidneys to selectively clear both urea and ammonia so they can be excreted in urine.

Dietary essential amino acids stimulate the synthesis of new muscle protein. Since nonessential amino acids make up approximately half of muscle protein, and consumption of an essential amino acid dietary supplement does not include the nonessential amino acids, the production of complete muscle protein requires that nonessential amino acids be derived in part from protein breakdown. As a result, nonessential amino acid concentrations, including alanine and glutamine, are reduced when you take an essential amino acid supplement. This imparts a positive effect on individuals with chronic renal insufficiency because a release of alanine and glutamine into the blood from muscle is correspondingly reduced. As a result of reduced flux of alanine and glutamine to the liver, the production of both urea and ammonia are lowered, which greatly helps uremic patients.

Thus, essential amino acid consumption stimulates muscle protein synthesis while lessening the burden on the kidney to excrete urea and ammonia. The devastating effect of the combination of anabolic resistance and reduced protein intake can be overcome with essential amino acids.

The relationships between muscle protein and amino acid metabolism, urea production in the liver, and urea excretion by the kidney are shown in the figures below. (Ammonia is not shown because it contributes much less than urea to the flux of nitrogen in the body.)

Amino acids and kidney disease are inextricably linked. The kidneys are responsible for excreting metabolic waste products, including urea and ammonia, which are the end products of amino acid metabolism. Kidney disease is characterized by the failure to effectively clear these and other compounds from the blood.

Since kidney disease necessitates a reduction in protein intake to minimize the burden of ammonia and urea on the kidneys, supplemental essential amino acids are even more important in kidney disease than in other catabolic states. The dosage should, therefore, be greater than in other circumstances to maintain a healthy nutritional status, and the supplement must contain all the essential amino acids and not just the branched-chain amino acids. Two 15-gram doses per day of essential amino acids are reasonable.

A Case Study

A noteworthy Johns Hopkins study published in the journal Kidney International confirmed the unique influence amino acids have on kidney disease, specifically on serum albumin levels. Your liver makes the protein albumin to help keep fluid in your bloodstream from leaking into other tissues.

Of the 47 patients studied, 29 were on hemodialysis and 18 were on peritoneal dialysis. On hemodialysis, the waste is filtered directly from the blood, and on peritoneal dialysis, toxins are removed through a soft tube in the abdominal wall that is replaced several times a day.

Patients were randomly prescribed either 5 amino acid capsules or 5 placebo capsules with meals 3 times a day for 3 months. Serum albumin levels were taken at the end of each month.

The hemodialysis patients who took the amino acid supplements had a 0.22 g/dl increase in serum albumin levels, but the peritoneal dialysis patients only had an average increase of 0.01 g/dL.

“We hope that this increase in serum albumin will result in better health and increased survival for patients treated with hemodialysis,” says Joseph A. Eustace, M.D., lead author of the study and an instructor of medicine at Hopkins.

By making sure the protein needs of CKD patients are met with amino acid supplements, secondary conditions such as metabolic acidosis, bone disease, and insulin resistance can be better prevented.

Amino Acids and Protein Nutrition for Cancer Cachexia

Virtually all forms of cancer induce a condition called cachexia, a weakening and wasting away of the body during serious illness. The effects of cancer cachexia have become recognized as a major factor in determining the effectiveness of cancer therapy and ultimately mortality. And amino acids are an important nutritional therapy for combating it.

There are many forms of cancer, from pancreatic cancer to non-small cell lung cancer to colorectal cancer. And each has specific and unique characteristics. However, virtually all forms of cancer, especially advanced cancers, induce a condition called cachexia—a weakening and wasting away of the body during serious illness that shouldn’t be confused with sarcopenia, which refers to the loss of muscle mass and function commonly seen with aging. While cachexia is known to occur during the course of a number of serious illnesses, including acquired immunodeficiency syndrome (AIDS), chronic obstructive pulmonary disease (COPD), and heart failure, when it occurs as a side effect of cancer, it’s known as cancer cachexia. And the effects of cancer-related cachexia have become recognized as a major factor in determining both the effectiveness of cancer therapy and, ultimately, mortality.

What Is Cancer Cachexia?

An international consensus regarding the definition of cachexia wasn’t reached until 2011, when a panel of experts convened for a formal consensus process.

According to the authors—including Kenneth Fearon and Stefan Anker—of the report, which appeared in The Lancet Oncology (Lancet Oncol), the definition of cancer cachexia that emerged was this: “A multifactorial syndrome characterized by an ongoing loss of skeletal muscle mass (with or without loss of fat mass) that cannot be fully reversed by conventional nutritional support and leads to progressive functional impairment. The pathophysiology is characterized by a negative protein and energy balance driven by a variable combination of reduced food intake and abnormal metabolism.”

The international panel also emphasized the importance of additional factors related to cancer cachexia, including tumor progression, systemic inflammation, reduced muscle mass and function, and psychosocial difficulties, and set forth a classification of cancer cachexia that included three stages:

  1. Precachexia
  2. Cachexia
  3. Refractory cachexia

In addition, and as noted in a 2011 systematic review, this wasting syndrome is associated with both metabolic changes in the body that render normal nutrition ineffective and cancer-related anorexia, or loss of appetite that reduces food intake and thus energy intake, which is why cancer cachexia is sometimes called cancer anorexia-cachexia syndrome.

Moreover, a 2015 study found higher levels of pro-inflammatory cytokines (like tumor necrosis factor) and lower levels of anti-inflammatory cytokines within the cancer tumors and adipose tissue (body fat) of patients with cancer cachexia.

Regardless of the name used, the end result is malnutrition and loss of lean body mass, which lead to muscle atrophy and changes in body composition. And this can have a number of detrimental effects, including:

  • Significant weight loss
  • Skeletal muscle loss
  • Loss of heart muscle
  • Weakness
  • Fatigue
  • Depression
  • Anxiety

Every single one of these consequences can impair a patient’s ability to recover from cancer.

A 2013 study conducted at a cancer center in Alberta, Canada, sought to determine the degree to which muscle loss contributes to cancer mortality. And results showed that, regardless of weight, cachectic patients (characterized by involuntary weight loss, muscle depletion, and low muscle attenuation, or decreased muscle quality) had a poor prognosis, while patients who maintained more lean muscle mass lived nearly 2 years longer.

A 2017 study determined that low muscle mass and muscle attenuation contribute to a poor outcome for metastatic breast cancer patients as well.

Is it possible to do anything about the devastating effects of cancer cachexia on muscle?

The answer is yes, but to determine the appropriate treatment, we must first understand what causes the onset of cachexia.

Unfortunately, this can be difficult because, at a molecular level, scientists don’t fully understand the precise mechanisms involved. However, we do understand, as demonstrated in a 2006 study by Vickie Baracos, that, at the physiological level, nutritional therapy is key to tackling cancer cachexia.

The Stress Response in Cancer

Cancer places the body under physiological stress. As a result, appetite is reduced and food intake falls. Thus, during the stress response, there’s a greater need than ever for amino acid nutrition.

And this is because amino acids are required to produce the new proteins needed to help battle the cancer—such as the proteins involved with immune function and the proteins in tissues and organs like the liver and brain, whose uninterrupted function is absolutely essential for survival.

While nonessential amino acids can be produced in the body, the nine essential amino acids must be obtained through diet. And since the body’s main reservoir of amino acids is muscle tissue, an insufficient quantity of these building blocks of life means that muscle protein starts to break down at an accelerated rate to maintain a steady supply of both nonessential and essential amino acids for the other tissues and organs.

Muscle is the primary tissue that can afford to lose some of its protein mass without affecting normal physiology. However, the stress response is adaptive for only a few days—continued loss of muscle protein for longer than that will begin to adversely affect many normal physiological responses. Thus, continued and accelerated loss of muscle protein is the physiological basis for the development of cancer cachexia.

Consequences of Malnutrition and Lean Tissue Loss

Conventional Treatment of Cancer Cachexia

Scientists and oncologists have been searching for a treatment for cancer cachexia for many years but have yet to produce a successful solution. The most current recommendations for treatment of cancer cachexia come from the European Society of Parenteral and Enteral Nutrition (ESPEN).

These recommendations focus on the early diagnosis of nutritional risk and call for the use of a variety of nutritional interventions as well as efforts to decrease inflammation and increase physical activity. Unfortunately, several factors may lead to significant problems implementing the ESPEN recommendations.

Although increased activity is the most effective way to reverse muscle protein breakdown, a cancer patient usually doesn’t feel like doing a lot of activity. And while reducing inflammation with nutrients (such as the omega-3 fatty acids found in fish oil) is useful for mild cases, the level of systemic inflammation in cancer cachexia is so great that dietary approaches often have little impact.

Further, the suppression of appetite seen in cancer cachexia limits how much adequate nutrition can actually be consumed. In fact, it’s often necessary to provide nutritional support via tube or intravenous feedings.

In addition, the normal effectiveness of dietary protein in reversing the breakdown of muscle protein is limited in cancer cachexia.

Anabolic Resistance and Cancer Cachexia

The term anabolism refers to the building up of muscle. This can be contrasted with catabolism, which refers to the breakdown of muscle via protein degradation.

Dietary protein is normally anabolic because it stimulates the production of new muscle protein. However, in cancer cachexia, muscle becomes resistant to the normal anabolic effect of dietary protein via a process called anabolic resistance.

A 2011 double-blind clinical trial published in the journal Clinical Nutrition (Clin Nutr) demonstrated that feeding a nutritional supplement containing proteins, carbohydrates, and fats designed specifically for cancer cachexia was completely ineffective in stimulating the production of new muscle protein.

The problem in anabolic resistance is that the molecular machinery in the muscle that must be triggered to initiate the process of protein synthesis is in an inactive state and can’t be activated by normal nutrition.

However, a high dose of the amino acid leucine can activate these intracellular factors.

For example, when a high dose of leucine was added to the nutritional supplement in the study described above, the supplement became an active stimulator of muscle protein synthesis.

Essential Amino Acids and Muscle Protein Synthesis

The effectiveness of a nutritional supplement that’s been enhanced with leucine for the treatment of cancer cachexia can be further increased by using a balanced mixture of essential amino acids to stimulate muscle protein synthesis.

A balanced mixture of essential amino acids—with a relatively high proportion of leucine—not only activates the initiation of muscle protein synthesis but also provides all the amino acids necessary for the synthesis of muscle protein since the body supplies ample quantities of nonessential amino acids.

Essential amino acids also have the great advantage of being effective in very small amounts. For instance, a dose as small as 3 grams can effectively stimulate muscle protein synthesis, thereby reversing the loss of muscle protein.

Do Essential Amino Acids Stimulate Tumor Growth?

The notion that providing nutrition to cancer patients feeds the tumor and accelerates growth has been kicked around for more than 40 years. And studies done on mice support this perspective, as feeding mice specific amino acids can indeed stimulate tumor growth. However, one must be extremely cautious when extrapolating results from mice to humans.

Experimental cancer in mice usually involves the implantation of tumors that become much larger, relative to body weight, than any tumor in humans. Further, mice have very little muscle. Thus, a big tumor without much muscle means that the tumor isn’t getting all the amino acids it needs for optimal growth from muscle protein breakdown.

Therefore, dietary amino acids can stimulate tumor growth in mice—but this doesn’t accurately reflect the response seen in humans.

In humans, muscle mass is large relative to tumor load, so muscle protein breakdown provides the tumor with all the amino acids necessary for rapid growth.

Consequently, dietary protein won’t stimulate tumor growth, as the tumor is already getting all the amino acids it needs. Rather, the absorbed amino acids will start to replete the muscle protein that’s been lost due to the cachexia response.

Essential Amino Acid Supplementation for Cancer Patients

The muscle wasting seen in cancer cachexia contributes directly to mortality and should be treated nutritionally. But because of anabolic resistance and decreased appetite, normal dietary intake is generally insufficient to combat the rapid loss of muscle.

Thus, treatment of cachexia that incorporates the use of dietary supplements containing essential amino acids, including a relatively high dose of leucine, is a reasonable approach to slowing the rate of muscle protein loss, preventing skeletal muscle wasting, and improving nutritional status, weight gain (and thus body mass index), performance status, response to cancer treatment, and quality of life.

The Best Animal Sources of Essential Amino Acids

Not all animal products contain the same amount of protein—and different cuts of the same meat contain different amounts of amino acids. Each tissue may have a different amino acid composition, determined by the specific function of the organ. So let’s find out what are the best animal sources of amino acids!

Without protein, we’d be a gelatinous mess. Protein gives structure and strength to the muscles, tendons, tissues, and organs in our bodies. This powerful macronutrient helps produce enzymes, chemicals, and hormones the body requires for virtually all biological processes. We need protein, and the building blocks that make them, to survive and thrive.

Animal products are considered the best sources of protein because they contain all nine of the building blocks of protein…the famous essential amino acids:

  • Histidine
  • Isoleucine
  • Leucine
  • Lysine
  • Methionine
  • Phenylalanine
  • Threonine
  • Tryptophan
  • Valine

Amino acids make up proteins by linking together in a specific sequence and forming their signature protein. Protein sources that contain the nine amino acids in adequate proportions are called complete proteins, and they are the highest quality protein sources from dietary protein.

Not all animal products contain the same makeup of amino acids, and different cuts of the same meat contain different amounts of protein. Each tissue has a unique amino acid composition, determined by the specific function of the organ.

Way back in 1943, researchers analyzed the amino acid makeup of protein in 10 muscle meats:

  1. Beef
  2. Veal
  3. Lamb
  4. Pork
  5. Chicken
  6. Turtle
  7. Codfish
  8. Salmon
  9. Frog legs
  10. Shrimp

And six beef organ tissues:

  1. Liver
  2. Kidney
  3. Brain
  4. Heart
  5. Stomach
  6. Lung

The results show that these various classes of animals do not differ widely in their amino acid composition—the only significant difference was found in the presence of lysine, an essential amino acid critical to immune system health. The organs had similar amino acid compositions to the muscle tissues, but with lower lysine contents.

The takeaway? It’s important to eat a varied diet of both animal- and plant-based protein to ensure adequate consumption of dietary amino acids. We’ll cover the differences between the two below, but first, let’s get clear on the best animal sources of amino acids, so you can be sure you’re providing your body with the protein it needs to live a strong and healthy life.

5 Best Animal Sources of Amino Acids

No matter what type of meat you eat—beef, chicken, or fish—it’s important to upgrade the quality in order to sustain the health gains. Processed meat like cold cuts, hot dogs, and sausage links that have been smoked, salted, cured, dried, or canned contain harmful chemicals and have been linked to chronic diseases such as hypertension, heart disease, bowel and stomach cancers, and COPD.

When choosing from the animal sources of protein below, opt for pasture-raised and grass-fed meats and animal byproducts to make sure you’re getting all of protein’s health benefits. When it comes to fishing, it depends on the fish: some fish are healthier sourced as wild-caught, while farm-raised fish can occasionally be a better choice.

1. Beef

Beef is a top-notch protein source, but the nutritional quality and quantity of saturated fats and amino acids depends on the cut and how the animals are raised. Steer clear of industrially raised livestock in favor of grass-fed animal sources.

The different parts of the cow also have different flavors; some are more tender and flavorful, while others are quite tough.

Round and back leg are the leanest cuts of beef, and they are perfect grilled. Lean cuts of beef provide about 31 grams of protein in each 3-ounce serving. A good rule of thumb is that the fattier the cut, the lower the protein content per gram. Hindquarters pretty much match the protein and saturated fat content of lean cuts of beef, and can be delicious when marinated overnight for enhanced flavor. The lower loin is a good source of protein and lower in fat, but tough, so it depends on your palate.

The quality of a protein food source depends not only on the protein and essential amino acid content, but also on its digestibility. Different cuts of beef not only have differing amounts of protein, but they also differ in terms of digestibility. Digestibility determines how much of the protein in beef actually gets into the body. For example, the digestibility of ground beef is greater than that of flank steak.

2. Pork

Pork is another good source of protein, but certain cuts contain a significant amount of fat. Ham comes from the leanest cuts of pork in the hindquarters and the lower half of the pig. There are 19 grams of protein and 2.2 grams of saturated fat in 85 grams of ham, while 85 grams of pork tenderloins contains 24 grams of protein and 1.3 grams of saturated fat.

3. Eggs

Just one egg has about 6 grams of protein. Egg whites might not be the best part of the egg in terms of flavor, but they are the leanest protein source. A single egg white contains 3.6 grams of protein and no fat. Egg whites house nearly half of all the protein in an egg, plus magnesium, potassium, and riboflavin, while the yolks contain many essential vitamins.

4. White Meats

White meats such as chicken and turkey are particularly rich in essential amino acids and contain less fat and cholesterol than red meat does. A 3-ounce serving of chicken or turkey breast has about 28 grams of protein. Chicken breast is the leanest source of chicken, but turkey is a better alternative if you’re concerned about consuming too much saturated fat—for every 85 grams of roasted turkey breast you’re getting 26 grams of protein and a saturated fat content less than 0.5 grams.

5. Shellfish and Fish

Shrimp and scallops contain all the essential amino acids. Eighty-five grams of shrimp provides 20 grams of protein and zero saturated fat, and 85 grams of steamed scallops contains 17 grams of protein and only 0.2 grams of saturated fat.

Fish is also an excellent amino acid-rich animal food. A 3-ounce serving of halibut, tuna, or salmon provides about 22 protein grams. Coldwater fish like rainbow trout contains amino acids and is also rich in omega-3 fatty acids, making it a win for your health. Eighty-five grams of this fish baked offers up 20 grams of protein with a saturated fat content of 1.3 grams.

How many grams of protein are in our favorite meats?

What About Plant Protein?

While animal protein certainly wins the gold star in amino acid makeup, we shouldn’t limit our protein consumption to animal sources. Red meat supplies a hearty helping of amino acids, but should be eaten sparingly due to its equally high supply of fat and cholesterol, which has been linked to diseases such as cardiovascular disease and cancer. The same can be said about dairy products, which are also high-protein sources. Aim to eat no more than 1 to 2 servings of dairy per day.

Filling your plate with low-fat, high-quality protein from plant sources such as legumes, seeds, nuts, and whole grains, lowers your risk of heart disease and type 2 diabetes and ensures you get all the essential amino acids your body needs.

How Much Protein Do I Need to Eat?

The amount of protein that we need depends on our weight. Per kilogram of body weight for an adult, the recommended protein intake is 0.8 grams daily, or a little over 7 grams for every 20 pounds.

  • A 110-pound person needs a minimum of about 40 grams of protein each day.
  • A 210-pound person needs a minimum of about 74 grams of protein each day.

It’s important to consider that these are the minimum targets for protein, and don’t reflect your individual weight, health, or fitness goals. If you are looking to build muscle mass for instance, your daily protein needs are substantially greater, and can easily be boosted with a protein powder supplement. Likewise, if you’re recovering from illness, injury, or surgery eating enough protein can be tricky and made easier with an amino acid powder blend.

If you’re looking to increase your protein intake without taking in unnecessary calories from the carbohydrates and fats found in dietary protein such as animal and plant foods, check out our amino acid blends scientifically formulated for health benefits like weight loss, weight gain, heart health, liver health, muscle growth and more!

Grow Older Gracefully with Anti-Aging Amino Acids

When it comes to aging, there’s one thing we know for sure—it happens. There are many preventative measures we can take to protect against accelerated aging and improve quality of life into our golden years. Nutritive support with anti-aging amino acids is one of the top ways to keep aging at arm’s length.

When it comes to aging, there’s one thing we know for sure—it happens. As for the exact mechanisms behind it, there are many theories. One theory is that our genes determine our longevity and how the aging process plays out in our lives. Other aging experts believe aging is the result of accumulated DNA and cellular damage over time—all those UV rays, free radicals, and destructive oxygen compounds taking their toll on skin, heart, brain, and overall health. Chances are, there are myriad contributors to aging. And there are also many preventative measures we can take to protect against accelerated aging and improve quality of life into our golden years. Nutritive support with anti-aging amino acids is one of the top ways to ensure you remain vital and vibrant as you grow older.

How Anti-Aging Amino Acids Rejuvenate Your Skin, Connective Tissues, and More

Often, the skin is the first place where unwanted signs of aging appear. Aging shows up on the skin first as fine lines, then as wrinkles. As we approach our 30s, our skin becomes drier. In our 40s, the aging process can begin to accelerate. Not only can your skin become markedly thinner while losing firmness and elasticity, but you may also begin to experience hair loss, thinning and weakening of the nails, and degradation of the connective tissue that allows your joints to function.

Anti-aging amino acids can help maintain smoothness and elasticity of the skin, strengthen connective tissue, and keep nails strong and hair lush.

If you’re seeking amino acid anti-aging supplements, you should pay particular attention to these six important amino acids: creatine, arginine, lysine, glutamine, alanine, and cysteine.

When it comes to aging, there’s one thing we know for sure—it happens. There are many preventative measures we can take to protect against accelerated aging and improve quality of life into our golden years. Nutritive support with anti-aging amino acids is one of the top ways to keep aging at arm’s length.

The Relationship Between Collagen and Amino Acids

Before delving into the specifics of how each of these amino acids can help you grow older gracefully, let’s explore the  relationship between collagen and amino acids, which is central to their anti-aging properties.

Amino acids form the protein collagen. Collagen makes up our bones, tendons, cartilage, connective tissues, and skin. It’s what keeps wrinkles away and, alongside elastin, supports skin elasticity.

When collagen production tapers off, as it does with age, our skin sags and succumbs to wrinkles, our joints and ligaments become less pliable and more stiff and sore, and our hair starts to thin. Certain amino acids can help increase collagen production, which in turn can suppress unwanted symptoms of aging.

While several amino acids are involved in boosting collagen production, glycine and proline are the two amino acids that make up collagen (along with the amino acid derivative hydroxyproline made from proline and lysine). Together, glycine and proline account for two-thirds of collagen protein. However, proline and glycine are nonessential amino acids that are rarely limiting for collagen synthesis. The limiting amino acid is the amino acid that is in shortest supply in relation to need. The rate of protein synthesis—how much collagen can be produced—is limited to the availability of the least abundant amino acid. Typically, the essential amino acids are rate limiting, even when they comprise a relatively small amount of the total amino acids in the protein.

Our Paleothic ancestors got plenty of glycine and proline because they ate pretty much all the components of meat, but these days, we tend to leave out the bones and tendons. Bone broth is a great way to increase your intake of these two amino acids. Bone broth is also a great source of arginine. While it is a good idea to ensure that your diet includes proline and glycine, keep in mind that healthy skin requires an abundance of all the essential amino acids to trigger the synthetic response in skin collagen.

The Top 6 Anti-Aging Amino Acids

1. Creatine

Creatine is made from three amino acids: arginine, methionine, and glycine. It is an important energy source for cells and can help stimulate the repair of cells and connective tissue. Creatine also plays a key role in skin metabolism.

As we age, collagen production and skin cell division decline at a steady rate. After age 20, collagen production decreases by 1.5% every year, and from 30 onwards our bodies’ ability to produce collagen and elastin, the proteins that give structure, strength, and elasticity to skin, is greatly limited. Whereas skin cells used to renew every 28 days, by the time we reach our 40s, skin cell turnover happens every 30 to 40 days.

Creatine helps skin cells repair damaged DNA and stimulates cells to produce more collagen and elastin. It also wraps cells in a film of water, thereby helping to shield cells from harmful substances as well as supplying much-needed moisture.

2. Arginine

The conditionally essential amino acid arginine occurs naturally in the human body, but production diminishes over time. This means that if you wish to continue to reap the benefits of this powerful amino acid, it can be quite helpful to incorporate arginine-rich supplements into your wellness  routine.

Arginine aids in the synthesis of protein and improves collagen production. At a cellular level, it helps cells to divide properly and ensures they don’t suffer premature apoptosis (cell  death). Arginine also offers a natural way to help revitalize human growth hormone.

Human growth hormone (hGH) is best known for helping the body build lean muscle mass and burn fat. Studies show it can also help elevate bone density, improve cardiovascular health, and boost collagen production in those with deficient levels. Increased levels of human growth hormone can be a boon for those who wish to preserve the youthful appearance of their skin, as research indicates it can increase skin elasticity and reduce the appearance of fine lines and age spots.

Human growth hormone injections are a mainstream medicine approach to increasing hGH levels, but they are expensive, inconvenient, and many experts recommend against the use of this synthetic approach as an anti-aging treatment.

Arginine acts as an hGH secretagogue, which is a substance that triggers the pituitary gland to release more human growth hormone. According to a 2010 scientific review published in the Journal of Advanced Research: “The demonstrated anti-aging benefits of L-Arginine show greater potential than any pharmaceutical or nutraceutical agent ever previously discovered.”

3. Lysine

Lysine, an essential amino acid that we must get from our diet, functions as a foundational building block for many of the proteins that make up the muscles and other internal structures. Because it’s not naturally produced by the human body, lysine must be obtained from a balanced diet or from supplements.

Lysine is arguably one of the most essential components in any nutrient-based approach to growing older healthily as it works to combat both internal and external damage associated with the aging process.

By ensuring adequate lysine intake, we increase the body’s production of carnitine, a specialized amino acid that plays a vital role in energy production by converting fatty acids to usable energy forms. In doing so, it helps lower cholesterol levels and stimulate collagen production. Lysine also contributes to the production of elastin, which alongside collagen, keeps skin looking firm and fresh.

High levels of arginine, however, may lower lysine levels in the body because the two aminos share common pathways, which is why taking arginine supplements can lead to unwanted side effects. When taking anti-aging amino acid supplements, it’s crucial to supplement with a complete essential amino acid formula that maintains the balance of amino acids in the blood. Working together in an appropriate balance, arginine and lysine have been shown to boost human growth hormone levels.

4. Glutamine

Glutamine, a nonessential amino acid, is the most abundant amino acid in the human body. A multitude of health benefits can be attributed to glutamine, including forming the cells that line the small intestine as well as those that form the immune system, contributing to the production of other amino acids, and functioning as metabolic fuel to power cells throughout the human body. As with arginine, however, glutamine production naturally declines with age, making supplementation beneficial. Increasing your glutamine intake can also help you weather periods of stress, during which the body craves more glutamine.

Glutamine gives skin its strength, elasticity, and firmness, and when levels start to diminish, skin starts to sag and wrinkle. By eating a glutamine-rich diet—plenty of kale, plain yogurt, walnuts, fish, turkey, spinach, lima beans, and whey protein—you can promote flexible, strong muscle tissue and skin. If you’re not getting enough glutamine, your body will take it from muscle and skin tissues.

If the load of your diet is meat or you drink a lot of coffee or smoke, you may be suffering from an acid imbalance, which can harm cells and tissues. Glutamine can help regulate the acid-base balance of your body by flushing out poisonous ammonia that is a byproduct of the kidneys’ filtering process. Glutamine lends a proton to an ammonia molecule. An acid is neutralized and an alkalizing bicarbonate is preserved.

5. Alanine

Though alanine, a nonessential amino acid, can be readily synthesized by the human body, adding supplemental alanine can increase the anti-aging benefits you experience.

Alanine helps to clear toxins released by muscle protein breakdown from the bloodstream, regulates glucose and cholesterol levels, and serves as an important energy source for the muscles and central nervous system. It’s second only to glutamine when it comes to concentrations in the blood.

The primary anti-aging benefits of alanine have to do with its ability to interfere with the glycation process. This process damages collagen, so by disrupting it, alanine protects the body’s natural stores of collagen.

Alanine also supports the process by which muscle tissue rebuilds itself, reduces fatigue, and improves sugar metabolism.

6. Cysteine

Cysteine is a nonessential amino abundant in beta-keratin, a major protein that makes up your hair, skin, and nails. Beta-keratin, in turn, is a rich source of sulfur. Connective tissue and cartilage depend on sulfur bonds for structure and stability. We’ve already explained how age decreases flexibility and firmness in skin and joints, and a lack of sulfur is a common culprit in these age-related symptoms.

One of the most important roles of cysteine is as a component of the antioxidant glutathione, which is used throughout the body to neutralize free radicals, diminish oxidative stress, and protect the immune system.

Cysteine and glutathione help to defend against age-related health conditions that have been linked to an accumulation of toxins, such as dementia and multiple sclerosis.

When it comes to aging, there’s one thing we know for sure—it happens. There are many preventative measures we can take to protect against accelerated aging and improve quality of life into our golden years. Nutritive support with anti-aging amino acids is one of the top ways to keep aging at arm’s length.

Amino Acids vs. Protein Powder: Which Supplement Should You Take?

While amino acids are the victor in the amino acids vs. protein powder debate, it’s not really an either/or situation. Whey protein and amino acids can work synergistically to produce superior results. Find out how!

If you’re interested in how sports nutrition can support your muscle growth goals, you almost certainly know that a diet rich in high-quality protein sources is a prerequisite for anyone working to build muscle. Given that amino acids are the building blocks of protein, it’s only logical that they would be just as crucial. While it may seem like amino acids supplements and protein powders serve the same purpose, that’s not quite accurate. So, in the amino acids vs. protein powder showdown, which contender triumphs?

Read on to learn more about the pros and cons of both amino acids and protein powder.

The Case for Protein Powder

Any dietician will tell you that consuming an optimal quantity of high-quality dietary protein is linked to myriad health benefits. Our bodies use protein for building muscle tissue as well as other tissues such as skin, hair, and nails. Some common protein sources include meat, fish, and poultry as well as vegan options like soy protein, legumes, and nuts.

If you’re not sure how much protein you should be getting each day, this article can help you calculate an appropriate intake based on both your weight and activity level. Athletes in particular can find it difficult to meet their body’s protein needs through diet alone, and protein powders can be a valuable resource for making up the difference.

There are many different varieties of protein powders on the market. In addition to checking the amount of protein per gram, it’s important to distinguish between single protein supplements and blended protein supplements. The former contain just one type of protein, for example, grass-fed whey or a plant protein like soy or pea. The latter contain a blend of two or more types of protein, which can lead to a sustained release of amino acids. The quality of the ingredients remains crucial to the efficacy of both types of protein powders (we’ll delve into the question of quality assurance more deeply in a later section).

Protein powders made with complete proteins such as whey or casein contain all nine essential amino acids (EAAs) your body requires for sustained muscle growth and recovery, among other bodily functions.

Each type of protein powder has its own unique profile. Whey protein, for instance, digests and absorbs quickly, making it a good pick for a post-workout protein shake. Casein protein, however, absorbs much more slowly, making it ideal for your final dose of protein before bed as the amino acids it contains will release steadily throughout the night, fueling muscle repair as you sleep.

The Case for Amino Acids

Amino acids carry out a range of vital functions in the body. Not only do they propel muscle growth, but they also contribute to the production of hormones, neurotransmitters, co-enzymes, and other important biochemical messengers, as well as encouraging wound healing and strengthening immune responses.

There are 20 amino acids necessary for human health and well-being. Nine are known as essential amino acids (EAAs) because the human body cannot produce them, so it’s essential that we supply them via our diet or supplements. As touched on in the previous section, proteins that contain all nine essential amino acids are called complete proteins.

Three of the nine essential amino acids—leucine, isoleucine, and valine—account for 35% of human muscle tissue. These power players, known as the branched-chain amino acids (BCAAs) have a major influence on muscle protein synthesis. Leucine has the most demonstrable impact, but it can only work to its full potential when ingested with the appropriate ratios of the other two BCAAs and the remaining EAAs.

In fact, a significant advantage amino acid powder has over protein powder is that amino acid mixtures can be formulated exactly as desired. Precise mixtures of amino acids can be produced that target specific metabolic issues. Dietary proteins as well as protein powder supplements contain a range of amino acids including both essential amino acids and nonessential amino acids, in varying concentrations. Consequently, they cannot reliably target a specific amino-acid related metabolic response.

It’s also important to note that free-form amino acids can be completely absorbed more rapidly than any intact protein, including whey protein. When you ingest a mixture of free-form essential amino acids, the corresponding peak concentrations are higher and are achieved more rapidly.

As with protein powders, it’s common to find both single amino acid supplements as well as blended amino acid supplements. Popular picks for single amino acid supplements include leucine and glutamine. Blended supplements may feature a few amino acids with notably desirable effects, like the BCAAs, or the full range of EAAs. You can typically find amino acid supplements in both tablet and powder form.

Amino Acids vs. Protein Powder: Which Supplement Should You Take?

Amino Acids vs. Protein Powder—The Bottom Line

Protein powders offer an efficient, cost-effective way to increase your total protein intake while providing the caloric fuel your body needs to complete and recover from challenging workouts. They can fuel your muscle-building efforts and fill in any dietary gaps you might have at the same time.

Amino acid supplements, on the other hand, can precisely target various metabolic and physiological processes far more precisely than protein powders can. They can also be absorbed and utilized much more rapidly, meaning you will see more dramatic results faster.

What’s the Best Boost for Muscle Protein Synthesis?

Whey protein is a “fast” protein, which means it is digested and absorbed at a faster rate than other dietary proteins. But free-form amino acids surpass the absorption characteristics of even the fastest protein. The result is that the metabolic response to free amino acid supplements often surpasses the maximal effect that can be achieved with intact protein such as whey, and often with a smaller dose.

The figure below illustrates the advantages of supplementing with free-form essential amino acid mixtures when it comes to spiking muscle protein synthesis. Participants supplemented with three different doses—3.6 grams, 6.7 grams, and 15 grams—of a balanced mixture of all the free-form essential amino acids. Researchers then compared the results to those produced by 15 grams of whey protein and to those of a partial essential amino acid mixture of only branched-chained amino acids (BCAAs). An amino acid powder supplement formulated with all essential amino acids is the clear muscle protein synthesis booster.

Amino Acids vs. Protein Powder: Which Supplement Should You Take?

We can see how the increase in muscle protein synthesis is more responsive to essential amino acids. The ratios of essential amino acids in amino acid powders can also be optimized. A properly formulated essential amino acid supplement can be 3 times as effective as a whey protein powder supplement.

Combining Amino Acids and Protein Powder for Optimal Results

While essential amino acids are more potent than whey protein, there are advantages to combining aminos with whey as part of a muscle-building amino acid powder supplement. Whey protein is digested over a longer time frame than free-form essential amino acids are, and, as far as intact proteins go, has a good balance of essential amino acids (about 45% of the total).

When you consume whey protein with essential amino acids, you prolong the beneficial effects of the aminos. So, while amino acids are the victor in the amino acids vs. protein powder debate, it’s not really an either/or situation. Whey protein and amino acids can work synergistically to produce superior results.

How to Check the Quality of Protein Supplements

The discerning customer knows what he or she wants, but the information provided about a product is often limited to the label on the package. Unfortunately, labels can range from uninformative to downright deceptive.

For example, it is not unusual for as little as 60% of the calories in a “pure whey protein” product to actually come from whey protein, with the balance of calories being comprised of carbohydrate and fat. The lesson is this: Buyer beware! Don’t just buy on the basis of product name. Dig deep into what the product actually provides.

Another labeling issue of considerable concern is how to figure out the relative proportions of different proteins in a protein mixture. Most supplements include some whey protein, as it is widely accepted as one of the highest quality proteins. However, because of cost and certain characteristics, other proteins are often included, such as soy and collagen.

Labeling rarely includes the proportion of each protein. Consequently, the true protein quality of some supplements is uncertain. Ingredients are listed in order of descending quantity, so the first ingredient listed should ideally be a high-quality protein such as whey.

Finally, it is the right of consumers to get what the product promises. Often, this is not the case. Spot-checking of nutritional supplements has revealed that the actual contents do not always match the labeling. There can be ingredients lurking in protein supplement products that aren’t even listed on the label.

For this reason, it is advisable to only buy supplements whose contents have been certified by an independent source, such as US Pharmacopeia. Barring that, at least check the website of the producer to determine if they have the appropriate certifications.

This issue is of particular concern for athletes who could be unwittingly consuming banned substances. Numerous cases of positive tests for banned substances have occurred because an ingredient was included in a supplement but not mentioned in the packaging. Although the industry has been making progress in cleaning up this problem, it still persists. Protein supplements are not regulated by the Food and Drug Administration, so the responsibility falls on the consumer to deal only with reputable suppliers.

Amino Acids for Insomnia: What Causes Those Restless Nights and Tips for Sweet Sleep

If you’re like many other adults, you’ve spent more than one night tossing and turning with sleeplessness. Insomnia impacts energy level, mood, and health. Amino acids can be helpful in treating insomnia.

If you’re like many other adults, you’ve spent more than one night tossing and turning with sleeplessness. According to the American Sleep Association, 30% of American adults have occasional insomnia, while 10% have chronic insomnia. Although many of us think that insomnia is just a side effect of modern life, poor sleep can lead to a number of health conditions, including heart disease, colon cancer, obesity, diabetes, stroke, and dementia. Thankfully, however, amino acids may be all you need to get the restful sleep you’ve been craving. So if you’re curious to learn how amino acids for insomnia can help you get a good night’s sleep, you’ve come to the right place.

What Causes Insomnia?

Insomnia is the most common sleep disorder in the United States. While many people experience occasional episodes of acute insomnia, which may last days or weeks, some deal with chronic insomnia, which may last for a month or more.

Whether acute or chronic, insomnia can be caused by a number of different factors, from an imbalance in brain chemicals to other sleep disorders, such as sleep apnea. In addition, conditions like anxiety and depression as well as lifestyle factors, such as watching television before bed, using stimulants like nicotine or caffeine, or sleeping in a room that’s too hot or cold, can all cause insomnia.

Additional factors that can increase your risk of insomnia include:

  • Stress: When you’re under stress, it can be difficult to fall asleep and stay asleep. Moreover, the release of stress hormones can make it difficult to reach restorative deep sleep, which can leave you feeling even more stressed when you wake up.
  • Poor sleep habits: Napping, getting into bed at a different time each day, and using your bed for working, eating, or computer or cell phone activity can all lead to insomnia.
  • Eating before bed: Eating a large meal before bed can make you feel too uncomfortable to fall asleep or cause acid reflux, which can lead to insomnia. Likewise, eating high-carbohydrate foods can cause a quick surge of energy when you need to be winding down. So if you eat anything before bed, it should be a light, protein-rich snack that stabilizes your blood sugar and doesn’t fill you up.
  • Sleep pattern disruptions: Disturbances to your circadian rhythm, or sleep-wake cycle, caused by odd work schedules or travel that takes you across time zones can lead to insomnia.
  • Medical conditions: Health problems like chronic pain, cancer, diabetes, heart disease, and asthma can all lead to symptoms of insomnia.
  • Medications: Certain medications, such as antidepressants, medications for asthma and high blood pressure, and over-the-counter cold and allergy medications that contain stimulants, may lead to insomnia.

Many people with insomnia rely on sleeping pills to fall asleep. However, these types of medications can have negative side effects, including daytime grogginess and an increased risk of falling. And getting into the habit of using conventional sleep aids to get to sleep every night brings with it a very real risk of addiction, which can make insomnia even worse.

However, supplying the body with the nutrients it requires can support a healthy sleep-wake cycle and help you get the better sleep you need.

Amino Acids for Insomnia

Amino acids are known as the building blocks of life because we must have them to create the proteins our bodies use for almost every biological process. And some amino acids have been found to be especially effective at creating the conditions necessary for healthy sleep. These are:

  • Gamma-aminobutyric acid (GABA)
  • L-theanine
  • L-tryptophan
  • Glycine

GABA

GABA is an amino acid that also acts as the primary inhibitory neurotransmitter of the central nervous system. This inhibitory action means that GABA is helpful in aiding relaxation and shortening the time it takes to fall asleep. In fact, a 2008 study found that levels of GABA are approximately 30% lower in people with insomnia.

In addition, a study from 2010 demonstrated that a combination of GABA and 5-hydroxytryptophan (5-HTP)—an amino acid that acts as a precursor of serotonin, a neurotransmitter that plays a role in both mood and sleep—can reduce the time it takes to fall asleep and increase both sleep quality and the amount of sleep achieved.

And if you’re interested in raising levels of GABA on your own, try exercising. A 2013 study found that vigorous exercise leads to increased levels of GABA, which helps explain why exercise is known to improve sleep.

L-Theanine

L-theanine is an amino acid that was first discovered in green tea in 1949. Like all amino acids, L-theanine works in concert with other amino acids, and it’s known to increase levels of GABA—as well as the neurotransmitters serotonin and dopamine. A 2019 study found that a combination of GABA and L-theanine works better than either alone to reduce sleep latency and improve duration of sleep. In addition, GABA and L-theanine were found to significantly increase both rapid eye movement (REM) and non-REM sleep.

L-Tryptophan

Like 5-HTP, the amino acid L-tryptophan also functions as a precursor of serotonin. Moreover, L-tryptophan is converted in the body into 5-HTP, which is then converted into serotonin. Interestingly, studies have shown that 5-HTP crosses the blood-brain barrier at a higher rate than L-tryptophan and may be even more effective as a dietary supplement.

Part of serotonin’s role in sleep has to do with the fact that it acts as a precursor of melatonin—the hormone that helps regulate your sleep-wake cycle. When levels of both serotonin and melatonin are low, sleep suffers. By increasing levels of serotonin in the brain, amino acids like 5-HTP and tryptophan help increase feelings of well-being and regulate sleep.

Studies have also shown that L-tryptophan can induce a state of subjective sleepiness and decrease the time it takes to fall asleep. And a study from 2018 found that L-tryptophan is not only helpful for sleep but can also aid conditions as diverse as autism, heart disease, chronic kidney disease, depression, inflammatory bowel disease, and multiple sclerosis.

Glycine

Like GABA, glycine acts as an inhibitory neurotransmitter and plays a role in promoting sleep. However, glycine has the added benefit of lowering body temperature, which makes falling and staying asleep easier.

In addition, a 2012 study found that glycine can significantly reduce fatigue and sleepiness in people experiencing sleep deprivation. Moreover, similar to 5-HTP and L-tryptophan, glycine helps increase serotonin levels and correct circadian rhythm disorders.

If you’re suffering from insomnia and interested in avoiding the potential side effects and risks inherent in pharmaceutical approaches and would like to begin a program of amino acid supplementation instead, it’s important to be aware that amino acids work best when used as part of a balanced formula that contains all essential amino acids.

So be sure to look for a supplement that provides a balanced supply of all essential amino acids while also emphasizing amino acids for insomnia. In this way, you’ll be providing your brain with the fuel it needs to create the perfect conditions for optimal sleep.

It’s also a good idea to remember that insomnia may be a sign of a more serious medical condition, so if your symptoms get worse or don’t improve, speak with your health care provider about additional treatment options.

Amino Acids for Insomnia: What Causes Those Restless Nights and Tips for Sweet Sleep

How Many Grams of Amino Acids Do You Need a Day?

The ideal daily dose of amino acids varies based on factors such as your physical size, body weight, lean body mass, activity level, and so on. Before exploring how those factors affect how many grams of amino acids you need in a day, let’s review why you need amino acids to begin with.

When it comes to how many grams of amino acids you need in a day the dose is generally referred to in gram amounts. How the body responds to essential amino acids depends on how many grams it gets. A dose of as few as 3 grams can stimulate muscle protein synthesis significantly.

That said, the ideal daily dose of amino acids varies based on factors such as your physical size, body weight, lean body mass, activity level, and so on. Before exploring how those factors affect how many grams of amino acids you need in a day, let’s review why you need amino acids to begin with.

Why You Need Amino Acids

It’s common to see amino acids referred to as the building blocks of protein. And in fact, all dietary protein sources (both animal and plant proteins) contain the same 20 amino acids. However, the proportion of amino acids varies from protein to protein.

Over the course of the day, your body utilizes and recycles substantially more protein than most people consume in a day. Amino acids can be reutilized to some extent, but it’s still crucial to ensure your body gets a good, steady supply of these vital compounds. Regardless of your age, according to the United States National Research Council Subcommittee on Recommended Dietary Allowances, “A continuous supply of dietary amino acids is required to replace these losses, even after growth has ceased.”

Humans can’t synthesize 9 of the 20 amino acids. What this means is that the only ones available to carry out the many vital tasks for which amino acids are responsible are the ones you absorb from your dietary protein intake. For this reason, those nine—histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine—are called the essential amino acids.

Three of the essential amino acids, isoleucine, leucine, and valine, belong to a subgroup called the branched-chain amino acids. They’re often singled out from other amino acids and are particularly popular among athletes because they’ve been shown to enhance exercise performance, reduce muscle soreness and improve recovery, revamp body composition, and activate muscle protein synthesis.

The 11 remaining amino acids are considered nonessential, not because the body does not need them just as much as the essential amino acids for muscle growth and other vital functions but because the body can synthesize them.

A further seven of these can become indispensable under certain circumstances, for instance, if a person has liver damage. Those are known as conditionally essential amino acids.

While different amino acids have their own unique traits and responsibilities, for optimal health and wellness, you’ll have to provide all 20 amino acids your body needs—and provide them in the appropriate concentrations.

How Many Grams of Amino Acids Do You Need in a Day?

When determining how much of a nutrient you need a day, it is customary to consider macronutrients in the diet (protein, carbohydrates, and fats) as a percent of total caloric intake. But when it comes to how many grams of amino acids you need in a day the dose is generally referred to in gram amounts. The number of calories in a pure essential amino acid (EAA) supplement, for instance, is insignificant in the context of total caloric intake, and for this reason supplements are generally sold in gram (g) units.

The Standard: A 3-Gram Dose of Amino Acids

How the body responds to EAAs depends on how many grams it gets. A dose of as few as 3 grams can stimulate muscle protein synthesis significantly. Consuming a 3-gram EAA supplement can generate almost 6 grams of muscle protein—the perfect balance of EAAs enables the muscle to incorporate every single one of the EAAs into protein. The body also reuses readily available nonessential amino acids to contribute to the total amount of protein produced.

While a 3-gram dose can be effective over time, the amount of muscle protein made from that small dose is limited to the amount of EAAs consumed relative to the size of the muscle mass. While the production of 6 grams of muscle protein from 3 grams of EAAs is impressive, it is not a large amount of new muscle protein when compared with total muscle mass.

Muscle mass can range from 25-80 pounds depending on your gender, size, and body type. Certain EAA benefits, such as the anti-inflammatory effects, are immediately activated with a dosage of 3 grams, but it will take some patience before you see the benefits in terms of muscle size and strength—at least a month of regular consumption, preferably twice per day, to achieve noticeable gains in muscle mass and function.

The Maximum: A 15-Gram Dose of Amino Acids

The amount of muscle protein produced in response to EAA intake increases linearly up to a dose of 15 grams. Quite simply, a bigger dose will give you a bigger response, but more than 15 grams is unnecessary. Also, as long as you wait at least 1 hour after one dose before taking another dose, you will get the same response to each of the multiple doses in one day.

So, there is a big range of possible doses of EAAs. The appropriate dose depends on your desired results and how fast you want to achieve them.

If you are on the smaller side and are seeking to support muscle health, a basic dose of 3 grams is reasonable. For example, a petite woman of around 105 pounds with about 30 pounds of muscle will get a robust response and over time see positive effects with a 3-gram dose of EAAs.

A young healthy man who weighs 200 pounds and has a muscle mass of about 80 pounds would be better off with a 6-gram dose of EAAs. (A 3-gram dose would be just 0.008% of the muscle mass, so 6 grams would be more appropriate in order to account for the larger muscle mass.)

Two doses per day, between meals, is optimal, but you will still get beneficial effects if you only take one dose per day.

In addition to your protein needs based on your body fat and muscle percentages, your preferred activities and goals will influence both the amount of amino acids you need in a day as well as the optimal timing for ingesting those amino acids. If your primary goal is to facilitate weight loss, and particularly if you’re restricting calories to do so, you’ll want to take 15 grams of amino acids 5 times daily. But those focused on aging healthfully should take 3-6 grams of amino acids once or twice a day between meals.

The important point to keep in mind is that EAAs are required nutrients with many roles in the body beyond acting as components of muscle protein. A small dose of 3 grams can have beneficial effects in a number of respects in addition to building muscle, such as encouraging fat loss, so even a large muscular man will benefit from a small dose. The activities in which one participates, and the desired results from the EAA supplement, are probably more important than a person’s size or physical makeup.

how many grams of amino acids in a day

How to Take Essential Amino Acid Supplements

EAAs can be consumed either as powder dissolved in water, as capsules, as a beverage, or a combination of all three.

EAA supplements usually contain amino acids and some flavoring. It is common that about 20-25% of the weight of a supplement is flavoring. When determining the right EAA dose for you, be sure you are using the weight of the active component of the mixture (i.e, the EAAs) and are not including the weight of the flavoring. If you are using a supplement that has a mixture of free EAAs and protein, add the EAA component of the protein to the amount of free EAAs to determine the dose you are consuming. For example, if you are using a supplement containing 3 grams of free EAAs and 1.5 grams of whey protein you’re consuming approximately 4.5 grams of EAAs, since whey protein is roughly 50% EAAs.

If you are taking EAA supplements because your regular diet falls short in meeting the recommended intake of high-quality protein, then, in addition to the between-meal doses, I recommend taking supplements with your meals to enhance the physiological effectiveness of the consumption of the incomplete protein food sources in your diet. The dosage with meals to make up for dietary deficiencies depends on how far short your diet falls of the goal intake of high-quality protein. In the case of a vegan diet, this could be up to 15 grams of EAAs with each meal to obtain optimal results.

Optimal nutritional supplementation with EAAs will help maintain an adequate supply of amino acids in the blood throughout the day to support various physiological functions without the interruptions that normally occur when food is not being absorbed. Best results are therefore obtained by taking an EAA supplement twice per day, between meals or before going to bed.

If you are still unsure how many grams of amino acids you personally need in a day, don’t worry about it. The beauty of essential amino acids is that there are no known adverse responses to a balanced formulation of EAAs, so you don’t have to be concerned that you are taking too much. A very small dose has proven benefits for stimulating muscle protein synthesis, so you likewise don’t need to worry that you are taking too small of a dose to elicit beneficial results. The recommended dosages are meant as guidelines; if you find successful results with a different dose, stick with it.

The Effect of Protein and Amino Acids on Bone Health

Most everyone recognizes calcium, vitamin D, and other minerals as key nutrients for bone health. What many people don’t know is that a significant part of bone in living humans is comprised of protein. Dietary protein and amino acids are as important for bone building as they are for muscle building.

A large part of our lean body mass is the skeleton, which includes all the mineralized bones and the structural and mechanical support of cartilage and tendons.

Most everyone recognizes calcium, vitamin D, and other minerals as key nutrients for bone health. What many people don’t know is that a significant part of bone in living humans is comprised of protein (20-30%!). Therefore, it is logical that dietary protein and amino acids are as important for bone building as they are for muscle building.

Similarities Between Muscle and Bone

There are many similarities between muscle and bone in terms of the way they function and the purposes that they serve. Just as muscle is a reservoir for amino acids that circulate in the blood and replenish other body proteins and chemicals, bone is the storage form for calcium and phosphorous, two minerals that are vitally important for many of the chemical reactions that occur in the body.

As with amino acids, the blood level of these minerals is tightly controlled and there is a complex system involving hormones and other chemical messengers to regulate the release and uptake of calcium and phosphorus from bone. This continual “remodelling” is analogous to muscle protein turnover, although a bit slower. It takes approximately ten years for the entire bone mass to turn over.

Another similarity between muscle and bone is the “use it or lose it” paradigm. Just as muscle atrophies with lack of physical activity, bone also weakens and loses density without mechanical stress and weight-bearing activity.

What Are Bones Made Of?

Unlike the bleached white, hollow, rock-hard bone you see on the anatomy lab skeleton, living bone contains connective tissues (such as the endosteum or periosteum), a network of nerves and blood vessels, with the marrow at the center. If you think about what bones are put through in the course of daily activities (in particular, sports or vigorous physical labor) then it makes sense that bones need to be very strong and somewhat flexible.

Bone is made of crystals of mineral bound to protein, a composite which provides both strength and resilience. Collagen, assembled as a structure of long thin rods that contain three intertwined protein chains, makes up a good amount of bone protein. Calcium and phosphate combine (termed hydroxyapatite) and then bind in an orderly manner to the collagen matrix. Other proteins in bone provide additional strength and also play a role in binding minerals during bone formation.

Of the 30% of bone composed of organic compounds, 90-95% is collagen. Individual collagen molecules contain three polypeptides of about 1000 amino acids per chain with a high glycine and hydroxyproline content. The amino acids arginine and methionine are also important cartilage-forming substances.

As with muscle, having all the amino acids (essentials aminos, in particular) available in the correct balance is important for optimal bone development and maintenance. Amino acids also influence bone metabolism indirectly due to their role in the synthesis of growth hormones and growth factors that are involved in bone development and remodelling.  

The Importance of Amino Acids to Bone Health

Protein and amino acids are clearly important nutrients for bone health. Despite the solid evidence supporting this statement, there is a lot of misinformation out there regarding the relationship between dietary protein (animal proteins in particular) and bone health.

Early studies showed that higher intakes of dietary protein were associated with increases in urinary calcium excretion. It was further proposed that animal proteins, rich in sulfur-containing essential amino acids, could “acidify” the blood, thereby leaching calcium from the bone to neutralize the acid. While this theory is still widely disseminated, particularly by proponents of plant proteins, the science has long since explained and moved beyond the long-standing dogma that animal protein consumption results in a mild acidosis promoting the increased excretion of calcium. The original investigators set out to determine the source of the increased calcium and found that the higher protein intake actually increased absorption of calcium in the diet, and that the increased excretion of calcium in the urine merely reflected that increase in calcium uptake.   

This observation helped to explain why, in other studies looking at people’s level of protein intake and bone status, there always appeared to be a beneficial effect of higher protein intake on bone health. In fact, in a different study in which women were fed dietary protein at and below 0.8 g/kg (the RDA), the low protein intake was associated with a reduction in intestinal calcium absorption and a condition called hyperparathyroidism. Secondary hyperparathyroidism occurs when the calcium level is abnormally low, so the parathyroid gland secretes more hormone to try to increase calcium blood levels. The long-term consequences of these low-protein diet-induced changes in mineral metabolism are not known, but such a diet could be detrimental to skeletal health. Recent epidemiologic studies demonstrate reduced bone density and increased rates of bone loss in individuals habitually consuming low protein.

Optimizing the Musculoskeletal System

It is important to recognize that the bones, joints, and muscles are the key parts of an integrated musculoskeletal system. The relationship between muscle and bone is essential for modelling and remodelling, processes that increase bone strength and mass.

We know that weight-bearing exercises serve to increase not only muscle strength but also bone strength, and even obesity or a high body weight provides a direct mechanical force on bones.

Osteoporosis is usually a concern as individuals age and the maintenance of adequate bone strength and density with aging is highly dependent on the maintenance of adequate muscle mass and function. Interestingly, from a diet and exercise perspective, many of the same factors that build strong muscles; amino acids, dietary protein, insulin growth factor, and testosterone, also positively affect bone. Strategies to optimize muscle mass, strength, and function provide the same benefits to bone.

Bones thrive on nutrient-dense diets and healthy physical activity.  Here are some specific strategies to optimize bone health.

  1. Calcium is obviously vital for bone health but so are some other mineralsmagnesium and phosphorus in particular.  
  2. Vitamin D is essential for proper bone growth and remodeling. Other trace nutrients that play a role in bone metabolism include copper, boron, iron, zinc, vitamin A, vitamin K, vitamin C, and B vitamins.
  3. Dietary protein and essential amino acids are extremely important for bone health and density since they are part of the building material for living bones.
  4. Low-protein diets and insufficient essential amino acids can also indirectly weaken bones by altering hormones that are responsible for regulating the retention and loss of calcium from bones.
  5. Weight-bearing exercise (running, tennis, basketball, etc.) helps develop strong bones. The mechanical force stimulates bones to grow denser.
  6. Resistance exercise makes not just strong muscles but also strong bones. The torque placed on the bone from the muscle pulling on it stimulates the bone to grow bigger and denser.
  7. Family history is a factor in your risk for osteoporosis. While we can’t change our genetic makeup, we can double down on healthy lifestyle behaviors during “peak bone-building years” (teens and young adulthood) to optimize bone mass and lay in good reserves for later on in life.

Most everyone recognizes calcium, vitamin D, and other minerals as key nutrients for bone health. What many people don’t know is that a significant part of bone in living humans is comprised of protein. Dietary protein and amino acids are as important for bone building as they are for muscle building.

Amino Acids and Muscle Recovery After Exercise

Amino acids and muscle recovery go hand in hand. You need all 20 amino acids that make up the proteins in your body for optimal muscle recovery. Without amino acid support, your body eats away at its own muscle tissue for energy. We’ve got the scoop.

If you’re a fitness enthusiast, you probably tend to focus much more on the doing—sprinting, lifting, contracting—than on the process of recovery. However, if you don’t allow your muscles to recover, you can’t perform, compete, or train at your best. For just as our brains process information and create and consolidate memories as we sleep, so, too, do our muscles resynthesize, recalibrate, and grow when we rest. But did you know that you can also accelerate muscle growth during recovery by boosting muscle protein synthesis with amino acid nutrition? If you’re interested in increasing both muscle mass and exercise performance, come with us as we explore the fundamental relationship between amino acids and muscle recovery.

What Happens to Muscle During (and After) Exercise?

Every time you engage in exercise your muscles aren’t used to, some muscle damage occurs. And whether you’re an endurance athlete or into strength training, this unfamiliar stress leads to microscopic tears in the muscles. You’ve probably noticed the discomfort this causes a day or two after a high-intensity workout. Known as delayed onset muscle soreness (DOMS), this post-exercise pain is the result of the tension muscles experience during eccentric (lengthening) exercises.

Believe it or not, these microscopic tears and the muscle protein breakdown they lead to have to happen if muscle strength and mass are to increase. When muscle fibers are damaged, satellite cells rush in to fuse the damaged fibers together, and this creates newer, stronger, and larger muscle fibers.

Think of satellite cells as stem cells for your muscles. Not only are these precursors to skeletal muscle cells made of protein—and therefore amino acids, the building blocks of protein—but they’re also essential for muscle repair after a workout. Moreover, they stimulate the production of more durable muscle, and this leads to better muscle function.

Amino Acids and Muscle Recovery

According to a 1995 study, muscle protein synthesis (the process of building muscle) is elevated by 50% 4 hours after high-intensity resistance training and by 109% 24 hours post workout. So for the next 24 to 48 hours after intensive exercise, your body needs plenty of protein-rich foods and the amino acids they contain to supply your muscles with the nutrients they need to grow in size and strength.

In other words, amino acids and muscle recovery go hand in hand. In fact, you need all 20 amino acids that make up the proteins in your body for optimal muscle recovery. Eleven of these amino acids are produced in the body, but nine are essential amino acids (EAAs), which means they must be consumed in the diet because they’re not produced in the body.

Increasing protein intake after a workout with the use of a balanced EAA supplement or even protein supplements, such as protein shakes or whey protein—which contain all the EAAs—is an effective way to activate muscle protein synthesis and aid in muscle recovery.

Increasing consumption of EAAs also stimulates reutilization of the 11 nonessential amino acids (NEAAs) for protein synthesis, thereby decreasing their oxidation and resultant increase in the byproducts ammonia and urea, which further aids muscle recovery.

What all this means is that providing your muscles with the amino acid nutritional intervention they require helps keep your muscles protected. The reason for this is that protein is used by the body for almost every biological process, and the majority of that protein is locked up in muscle tissue. So if the availability of amino acids to rebuild the protein lost during muscle breakdown is limited, not only does muscle protein synthesis suffer, but your body also has no choice but to use its own muscle to keep the rest of the machine running.

Branched-Chain Amino Acids and Muscle Recovery

Branched-chain amino acid supplementation has become popular among bodybuilders and other workout buffs to help increase athletic performance. On the face of it, this makes sense, as branched-chain amino acids (BCAAs)—leucine, valine, and isoleucine—make up nearly 35% of muscle tissue and are a source of fuel for the muscles.

However, while this may accelerate recovery from muscle soreness, BCAAs are limited in their ability to stimulate muscle protein synthesis. This is because all the EAAs are required for a complete protein to be produced. In fact, a recent study demonstrated that taking BCAAs alone has either no effect or only a minor one on the rate of muscle protein synthesis.

Why is this?

Research has shown that the availability of all the EAAs determines the rate of muscle protein synthesis. So even if you’re consuming a BCAA supplement after your workout, the rate of muscle building is still going to be determined by how many of the other EAAs are present. This is because you can’t make a complete protein out of just three amino acids, so unless you’re also getting enough of the other six EAAs, the effectiveness of BCAAs will be limited.

In addition, an excess of BCAAs has been shown to disrupt levels of neurotransmitters in the brain. In fact, a 2013 study found that BCAA supplementation, when used in isolation, lowers levels of several important neurotransmitters, including catecholamines, which are necessary for enhanced athletic performance. So to get the most out of your exercise routine—and your muscles—you must consume BCAAs as part of a balanced mixture of all the EAAs.

However, even though consuming both protein and amino acid supplements after exercise can provide important benefits, it’s important to realize that they’re merely supplements to your regular diet. If you really want to give your muscles the nutritional support they need, focus on refueling your body after your workouts with foods that are abundant in amino acids.

Consuming between 0.5 and 0.9 grams of protein per pound of body weight should provide you with the right amount of amino acids to help increase your muscle mass and improve your athletic performance.

Foods high in amino acids

Amino Acids for Weight Loss: Boost Your Metabolism!

We all know the importance of diet and exercise for weight loss. There is, unfortunately, no magic weight-loss pill. There are, however, some pretty miraculous organic compounds that prime your body for weight loss and help boost your metabolism. We’ll give you one guess what they are!

We all know the importance of diet and exercise for weight loss—along with a sustained commitment to losing weight and keeping it off. And there is, unfortunately, no magic weight-loss pill that can help us shed the pounds and keep them off for good. But there are some pretty miraculous organic compounds that not only prime your body for weight loss but also help boost your metabolism. And these little building blocks of protein are completely safe and natural too. So come with us as we explore amino acids for weight loss and discover the many ways they can support your body’s metabolism and help you reach your weight management goals.

Amino Acids and Metabolism

Our bodies are constantly burning carbohydrates, fats, and proteins to provide the energy our cells need to perform the thousands of biochemical reactions that are continuously taking place throughout the day.

The sum total of the energy utilized by all these reactions is called the basal metabolic rate—the body’s rate of energy production when it’s at rest and not actively digesting food.

Because the basal metabolic rate is determined when the body’s at rest, the best time to measure the rate is when you’re sleeping (but since that’s not really practical for most of us, there are a number of online calculators available that can help you estimate your personal basal metabolic rate).

What’s more, the same basic metabolic functions that determine the basal rate of energy expenditure are also going on when the body’s active.

So, by adding the basal rate—which occurs continuously—to the amount of energy expended during daily activities, it’s possible to determine the body’s total metabolic expenditure (thankfully, there are online calculators that can help you measure this too).

Granted, this is all rather technical, but it helps us illustrate the fact that weight-loss promotions and articles that feature the appealing words “boost your metabolism” are really just saying, “Increase your basal metabolic rate.”

Here’s how it works: if your basal metabolic rate is greater than the number of calories you consume in a day, you’ll lose weight.

To express this in a slightly different way, if you can rev up your basal metabolic rate (i.e., boost your metabolism), you’ll lose body weight even if you maintain the same caloric intake—which is great news for those of us who don’t fancy eating a lower calorie diet.

There are two major contributors to the body’s basal metabolic rate:

  1. Reactions involved in maintaining a proper balance between sodium and potassium levels in the blood and inside the cells and reactions that use energy, such as those that make glucose
  2. The energy cost of protein turnover

Although it’s difficult to do much about the first, you can definitely increase the rate of protein turnover and thus boost your metabolism.

What Is Protein Turnover?

Protein turnover refers to the process by which the thousands of proteins in the human body are continuously created and broken down.

Energy, in the form of adenosine triphosphate, or ATP, fuels protein turnover—both the process of tearing protein down and the process of building it back up. Anywhere from one third to one half of our basal energy production is used to fuel protein turnover.

But the exact amount of energy used for protein turnover depends on how much muscle you have (the amount of protein in the rest of the body is pretty constant between individuals) and how fast muscle protein is turning over.

So the most effective way to boost your metabolism—and therefore your fat-burning capability—is to increase your muscle mass.

A 10-kilogram difference in muscle mass, with all else staying constant, equates to about a 35,000-kilocalorie difference in energy expenditure over a year.

And since about 3,500 kilocalories is stored in 1 pound of body fat, a 35,000-kilocalorie difference in energy expenditure translates to a gain or loss of 10 pounds of body fat over the course of a year.

What’s the Best Way to Build Muscle Fast and Increase Muscle Protein Turnover?

If you want to increase muscle protein turnover and build lean muscle fast, then incorporating exercise and protein/essential amino acids (EAAs) into your routine is absolutely essential.

Exercise increases muscle protein turnover for many hours after a workout and can, over a period of time, help contribute to both muscle growth and muscle mass. However, don’t expect major changes in muscle mass from exercise alone because you must increase the amount of protein and EAAs you consume to significantly affect mass.

So increasing dietary protein/EAA intake—whether through food sources, protein supplements like whey protein, or supplemental amino acids—is the key to boosting basal metabolic rate. Doing so will stimulate muscle protein turnover and increase muscle mass over the long term.

Dietary protein—and EAAs in particular—stimulates muscle protein turnover in two respects.

First, amino acid supplements have been shown to increase the basal rate of muscle protein turnover—which means that more energy is used to fuel the increase in protein turnover, thereby giving a persistent “boost” to your metabolism.

And this can have a positive impact on both weight loss and body composition. Check out the results in the figure below.

Basal muscle synthesis

Second, increased dietary protein and EAA intake helps boost metabolism and promote fat loss by influencing what’s known as diet-induced thermogenesis.

The body’s metabolic rate goes up about 10% for a couple of hours after eating a meal that contains dietary protein or consuming an EAA supplement. The exact amount of the increase depends on how much protein you eat with the meal or how many grams of EAAs you take. This response has been studied for many years and is called diet-induced thermogenesis.

Diet-induced thermogenesis refers to energy lost as heat after you eat protein. This process is only activated by dietary protein or EAAs, as neither dietary carbohydrates nor fats have much effect on metabolic rate.

However, when you consume dietary protein or an EAA supplement, your metabolic rate increases because energy is used to digest the protein and absorb the amino acids.

Therefore, eating a meal that contains dietary protein or taking an EAA supplement increases the metabolic rate by stimulating the rate of protein synthesis in the body, particularly in muscle, since the process of protein synthesis requires energy.

In addition, diet-induced thermogenesis of dietary protein actually lessens the caloric impact of protein.

Calories are classically determined by combusting a food source in a device that measures the amount of energy released. In the case of protein, 4 kilocalories per gram is normally released by combustion, so the caloric equivalency of protein is traditionally considered 4 kilocalories per gram.

This means that you can calculate how many protein calories are in a meal by multiplying the number of grams of protein by 4 kilocalories per gram.

However, since the digestion of protein increases the body’s metabolic rate by approximately 10%, the net caloric intake from the protein component of the meal is actually 10% less—or 3.6 kilocalories per gram—than the value you’d get by following the traditional approach.

So why not just stimulate diet-induced thermogenesis with dietary protein?

Because consuming EAAs increases protein turnover more than any dietary protein can, so EAAs therefore have a greater impact on diet-induced thermogenesis. Take a look at the following figure.

energy expenditure

It requires less work for EAAs to be absorbed by the intestines, so on a gram-per-gram basis, it may take less energy for the body to digest them than it does intact protein.

Even so, the consumption of EAAs actually stimulates protein synthesis about three times more than the consumption of intact protein does—thus leading to a greater increase in diet-induced thermogenesis.

Branched-Chain Amino Acids and Weight Loss

The branched-chain amino acids (BCAAs) leucine, isoleucine, and valine are a special group of EAAs that are known to have a direct impact on metabolic health.

Interestingly, although science has known for decades that blood concentrations of BCAAs are elevated in individuals with type 2 diabetes, the link between levels of BCAAs and the development of insulin resistance is not what it may initially seem.

In fact, the theory that dietary BCAAs are somehow to blame for the impaired glucose metabolism that leads to diabetes is contradicted by numerous studies over the past 20 years that have shown that supplementing with BCAAs can improve insulin sensitivity, and that increased concentrations of leucine, in particular, may actually improve blood sugar control.

Because people with insulin resistance and metabolic syndrome—a related group of conditions that includes obesity, insulin resistance, and high blood pressure and cholesterol levels—have greater difficulty losing weight, you might then assume that increased consumption of supplemental BCAAs could be helpful with weight loss.

And while the connection between BCAAs and weight loss has not been studied as thoroughly as the connection between BCAAs and insulin resistance, the research that has been performed on humans would indicate that your assumption is indeed correct.

For example, no human studies have thus far demonstrated any gains in body fat with consumption of BCAAs. In fact, just the opposite has been shown, with current research indicating that a calorie-restricted diet that’s high in BCAAs may actually lead to both greater fat loss and improved muscle retention.

Why Use Amino Acids for Weight Loss Instead of Drugs?

Although a number of both over-the-counter and prescription-based medications are currently being marketed as weight-loss aids, these types of drug-based approaches come with potential negative side effects, some of which may be severe.

By contrast, the stimulation of protein synthesis that occurs after ingesting EAAs is an entirely natural biological process without any known adverse effects. Moreover, long-term consumption of EAAs has been proven to result in a number of health benefits—advantages that aren’t seen with drug therapy.

Yet it’s important to keep in mind that protein synthesis can’t occur unless all EAAs are present in their optimal amounts. So to ensure you’re getting the most out of amino acids for weight loss, always look for a formula that includes a balanced supply of all nine EAAs.

4 Benefits of Amino Acids for Weight Loss