Independent education resourceInformation here does not replace care from a qualified health professional.
Peptide Therapy GuideClear peptide education

Educational guide

Collagen Peptides – Uses, Side Effects, and More

6 mins read Overview: Collagen is a dietary supplement that is available over the counter. Most collagen products are made from animals or fish. People often take collagen for skin and joint health, but its benefits are not well defined. Collagen is usually we

Written by Peptide Therapy Guide Editorial Team
For education only

This guide cannot diagnose a condition or recommend a personal treatment plan. Discuss medical questions with a qualified professional.

6 mins read

Overview: Collagen is a dietary supplement that is available over the counter. Most collagen products are made from animals or fish. People often take collagen for skin and joint health, but its benefits are not well defined. Collagen is usually well tolerated. Before taking collagen, make sure to tell your health care provider about any health conditions you have or medicines you are taking.

What is collagen used for?

Collagen is used for many different reasons, but its benefits are not well defined. Some common reasons that people use collagen include the following.

Note: The FDA has not reviewed collagen for safety and effectiveness. Learn more about dietary supplements here.

How does collagen work (mechanism of action)?

Collagen is the most common protein found in your body. It is important for the structure and health of your joints, tendons, ligaments, bones, hair, skin, and nails. Your body makes collagen from the proteins found in your diet.

There are many different types of collagen in your body, each with its own unique structure. Collagen types 1, 2, and 3 all play an important role in the structure of your skin, joints, and bones. Most collagen products contain one or more of these three types of collagen.

As you age, your body makes less collagen. This can make your skin less elastic and your joints stiffer. Taking collagen can help boost your collagen levels, so it is sometimes used to help with aging skin, bone health, and joint problems. Some people report that their skin and joints feel healthier after using collagen. But its benefits for reducing the impact of aging are not well defined. It is possible that certain types of collagen may work better for different uses, but the research is not clear.

Collagen is a very large protein. When you take collagen by mouth, your body may not absorb it very well. Collagen is also too large to be absorbed when applied to your skin. Because of this, many collagen supplements contain collagen that has been broken down into smaller pieces, called peptides. Collagen peptides are made by a process called hydrolysis, so they are sometimes called hydrolyzed collagen or collagen hydrolysate. Your body can use these smaller pieces to make collagen and increase collagen levels. But the benefits of collagen peptides are not well defined.

How should I store collagen?

You should store collagen according to the product label. Most dietary supplements should be kept in a cool, dry location that is out of the reach of children and pets and not in direct sunlight.

What are the most common side effects of collagen?

Collagen seems to be well tolerated. Tell your health care provider if you have any side effects that bother you.

There may be side effects of collagen that are not listed here. Contact your health care provider if you think you are having a side effect of a supplement. In the U.S., you can report side effects to the FDA at www.safetyreporting.hhs.gov or by calling 888-SAFEFOOD (888-723-3366). In Canada, you can report side effects to Health Canada at www.health.gc.ca/medeffect or by calling 866-234-2345.

What are the serious side effects of collagen?

While less common, the most serious side effects of collagen are described below, along with what to do if they happen.

Severe Allergic Reactions. Collagen may cause allergic reactions, which can be serious. Stop using collagen and get help right away if you have any of the following symptoms of a serious allergic reaction.

  • Breathing problems or wheezing
  • Racing heart
  • Fever or general ill feeling
  • Swollen lymph nodes
  • Swelling of the face, lips, mouth, tongue, or throat
  • Trouble swallowing or throat tightness
  • Itching or skin rash
  • Bumps on the skin called hives, which can be red, pink, white, or brown depending on your skin tone
  • Nausea or vomiting
  • Dizziness, feeling lightheaded, or fainting
  • Stomach cramps
  • Joint pain

Who should not use collagen?

Allergies to Ingredients. People who are allergic to any of the following should not use collagen.

  • Collagen
  • Collagen hydrolysate
  • Collagen peptides
  • Hydrolyzed collagen
  • Any of the ingredients in the specific product

Your pharmacist can tell you all of the ingredients in the specific collagen products they stock.

What should I know about collagen before using it?

Collagen is a dietary supplement. It cannot be marketed to treat or cure a disease.

Read and follow the directions on the specific product you are using, or use it as recommended by your health care provider.

Keep collagen out of the reach of children.

Collagen comes from animal or marine sources. Most collagen dietary supplements come from chicken, pigs, or cows. Some collagen products come from fish skins. If you have any dietary restrictions, it is important to read the product label carefully to understand where the ingredients came from.

Some dietary supplements are labeled as vegan collagen, but these products do not actually contain collagen. Collagen is hard to make in a lab and is only found in animals and fish. Instead, these products contain ingredients that your body needs to make collagen, such as the amino acids that make up collagen protein. Some products contain “collagen boosters,” which are chemicals such as vitamin C, zinc, and copper; these may help your body make more collagen. It is not clear if any of these ingredients can boost your collagen levels. Read the product label carefully to understand which ingredients it contains.

If you are using collagen powder, use a proper measuring device to measure the powder, such as the device included with the product. Read the label carefully and measure the amount stated on the label. Mix the powder with a glass of liquid, such as water or juice.

The FDA has not tested collagen products to confirm that they contain the ingredients stated on their labels. Some dietary supplements have been tested by third-party organizations to confirm that they contain the ingredients listed on their labels and do not contain any harmful chemicals. Learn more about how to choose a safe dietary supplement product here.

What should I tell my health care provider before using collagen?

Tell your health care provider about all of your health conditions and any prescription or over-the-counter (OTC) medicines, vitamins/minerals, herbal products, and other supplements you are using. This will help them know if collagen is right for you.

In particular, make sure that you discuss any of the following.

Fish Allergy. Some collagen products are made from fish skins. If you are allergic to fish, read the product label carefully and talk to your health care provider before taking collagen.

Pregnancy. It is not known if or how collagen could affect pregnancy or harm a fetus. Tell your health care provider if you are pregnant or plan to become pregnant.

Breastfeeding. It is not known if collagen passes into breast milk. Tell your health care provider if you are breastfeeding or plan to breastfeed.

Does collagen interact with foods or drinks?

There are no known interactions between collagen and foods or drinks.

It is unknown if drinking alcohol will affect collagen.

Does collagen interact with medicines (drug interactions)?

There are no known interactions between collagen and medicines. Always tell your health care provider about any prescription or over-the-counter (OTC) medicines, vitamins/minerals, herbal products, and other supplements you are using.

The interactions between collagen and medicines are not fully understood. As with most dietary supplements, the research on drug interactions with collagen is incomplete. Always check with your health care provider before taking collagen with any medicines.

What should I do if I accidentally use too much collagen?

If you or someone else has used too much collagen, get medical help right away, call 911, or contact a Poison Control center at 800-222-1222.

Collagen is usually made from chicken, cows, pigs, or fish. Read the product label closely and speak with a health care provider about how to take collagen safely. Do not take double or extra doses, even if you miss a dose.

Connected reading

Helpful context for this guide

Source-derived material selected through this article’s indexed topics.

Related questions

01Are Protein Drinks Safe to Use Every Day?

However, Zenker cautions that relying too heavily on shakes “can crowd out other important nutrients your body needs, like fiber, healthy fats, and antioxidants from whole foods, as well as the physical and social experience of eating real meals.” A qualified healthcare professional can help you choose a product that supports your health goals without compromising safety, ensuring that it fits within your calorie, carbohydrate, protein, and nutrient needs.

Source: www.everydayhealth.com ↗
02What are the side effects of collagen supplements?

Possible adverse effects include mild diarrhea, a heaviness in the abdomen, and a rash. There may be interactions with other drugs. However, research has not yet shown which ones.

Source: www.medicalnewstoday.com ↗
03A peptide identified in a fungus found in northern European pine forests possesses as much power as penicillin as well as vancomycin, according to an international team of researchers.

Reporting in the October 13 issue of Nature, a team from Denmark-based biotech company Novozymes, and researchers from Georgetown University Medical Center and the David Geffen School of Medicine at UCLA, say they have isolated "plectasin," the first defensin ever found in fungi. The research was performed at Novozymes laboratories in Denmark. Defensins are peptides, miniature protein molecules that are produced by a wide range of animals to protect themselves against infection. Humans have defensins in their white blood cells and in their skin, for example, but it is believed that this new fungal defensin, plectasin, is more potent and targets certain bacteria more specifically. Indeed, when plectasin was tested in the laboratory and in animals, it proved to be highly effective against the bacteria Streptococcus pneumoniae, and Streptococcus pyogenes, including strains that are now resistant to conventional antibiotics. These bacteria are responsible for such diseases as meningitis, community-acquired pneumonia, strep throat, life-threatening sepsis, and flesh destroying skin infections. The discovery of plectasin has implications for the development of defensins as a treatment against many common, and deadly, infections, and may initiate a new era of antibiotic discovery and development, said study co-author Michael Zasloff, M.D., Ph.D., Professor in the Departments of Surgery and Pediatrics at Georgetown University Medical Center. Zasloff says that the field of antibiotic development has not changed much since 1929 when Alexander Fleming realized that the fungal "bread mold" Penicillium, which had landed by chance in a Petri dish produced a substance that eliminated colonies of staphylococcal bacteria. "Most antibiotics used by humans are produced by fungi and certain soil bacteria," he said. "Using our existing tools of discovery, we have failed to uncover any new classes of antibiotics from these sources over the past decade. However, by utilizing a new genetic approach that allowed the team to discover plectasin, we now know that a whole class of antibiotics has been overlooked." "This finding (plectasin), and the existence of about 200,000 additional species of fungi, opens up a vast universe to explore for novel peptide antibiotics," said co-author Robert Lehrer, M.D., Distinguished Professor of Medicine at the David Geffen School of Medicine at UCLA. Plectasin, if proven safe and effective in humans, could be on the market by 2012, said Lehrer. Zasloff and Lehrer are known internationally as experts in antimicrobial peptides - the class of antibiotics that plectasin falls within - and in this study they collaborated with Novozymes, a Danish biotech company that led the research. Zasloff and Lehrer are the only two scientists from U.S. universities on the team of 20 researchers who co-authored the research paper. All life forms have to defend themselves against microbial invaders - bacteria, fungi, viruses - and to do this, they produce antimicrobial defensin peptides. In humans, defensins are made by specific white blood cells and immune cells that later engulf foreign invaders, and by the skin and mucous membranes, in order to kill microbes before they invade protective barriers. Researchers believe that fungi have a similar system of defense, especially since these plant-like organisms live off rotting matter, said Zasloff. "They must compete with other organisms, like bacteria and viruses, which also want to consume the same meal. In addition, they need to defend themselves from being eaten by the microbes which surround them." But he said no one had been able to find defensins in fungi using traditional research techniques, which involved growing fungi in liquid cultures and then testing the culture to see if it contained any antibiotic molecule. The research team instead used the latest genetic science to search for the defensins they thought fungi must have. Selecting the Pseudoplectania nigrella species of fungus may have been serendipitous, Lehrer said, but the Novozymes team used state-of-the-art biotechnology to intercept ,and interpret its genetic messages and exhibited tremendous skill in producing plectasin efficiently, economically, and in large amounts." "I started working on antimicrobial peptides over three decades ago, said Lehrer, and my laboratory first described human defensins in 1985. So, the discovery of plectasin makes me feel like a grandfather." Further examination revealed that this defensin, plectasin, resembles defensins found in spiders, scorpions, dragonflies and mussels - thus suggesting that the defensins found in insects, molluscs and fungi arose from a common ancestral gene, the researchers say. Based on this information, the scientists now believe that defensins appeared in living things more than a billion years ago. The investigators then turned to the National Center for Antimicrobials and Infection Control, the Danish equivalent of the U.S. Centers for Disease Control, to test plectasin in the laboratory for antimicrobial activity against a broad spectrum of bacteria. It showed potent activity against several species of Gram-positive bacteria, and was especially active against S. pneumoniae (the leading cause of pneumonia), including all known clinical strains and those that are now resistant to conventional antibiotics. "That is important because increasing bacterial resistance to conventional antibiotics threatens the future of many antibiotics in current use," Zasloff said. "In mouse studies, plectasin showed extremely low toxicity, and was as effective as vancomycin and penicillin in curing the animals of experimental peritonitis (inflammation of the lining of the abdominal cavity, which can be deadly) and pneumonia caused by S. pneumoniae, the researchers report. "Although the precise mechanism by which plectasin exerts its antimicrobial activity is still under investigation, it may work by a mechanism that is very different from traditional antibiotics, Zasloff said. "As a group, defensins exhibit activity against many types of bacteria, fungi, protozoa, and even viruses. It is entirely possible that fungal defensins will be discovered that could be developed against all of these human pathogens," Zasloff added.

Source: www.news-medical.net ↗
04What is nisin?

Some bacterial species produce antimicrobial peptides known as bacteriocins that have been used in the food industry as preservatives. For example, nisin, which is produced by Lactococcus lactis, has broad-spectrum bactericidal activity and has been used as a food preservative throughout the world. Nisin is effective in controlling Gram-positive bacteria such as Clostridioides difficile. In combination with other compounds like ethylene diamine tetra-acetic acid and cinnamaldehyde, nisin has been effective in controlling enterotoxigenic Gram-negative bacteria such as Escherichia coli. Previous studies have used chicken and mouse models to demonstrate the in vivo efficacy of nisin on the microbiome, whereas nisin efficacy has been proven in ex vivo experiments on the human microbiome. To date, no studies have assessed the in vivo effects of nisin in large mammals.

Source: www.news-medical.net ↗
05How do these peptides act?

These peptides, like the parent compound AC253, acted as antagonists at the AMY receptor. They were also resistant to protein breakdown, and crossed the blood-brain barrier easily when injected into the abdominal cavity, to localize in the hippocampus, which is crucial in memory. These peptides protected the brain against beta-amyloid injury, and normalized the AD-associated impairment of the memory-associated long-term potentiation of nerve impulses in the hippocampus. They improved memory testing results, and reduced the level of inflammation in the brain. These effects appear to be mediated via the blockade of AMY receptors. For instance, inhibition of microglial AMY receptors reduce the activation of the inflammasome NLRP3. This reduces the secretion of inflammatory chemicals in the surrounding brain tissue, which offers another mechanism for lower amyloid production. In addition, these peptides increase the rate of outflow of amyloid beta from the brain, which also contributes to a lower level of amyloid after treatment. These marked changes all occurred within a relatively short span of treatment. A very important additional finding was that treatment with these peptides brought about improvement in mice which were showing signs of well-established AD in the brain as well as in their behavior. This is unique in that most therapies fail to affect the progress of AD once it has begun to manifest clinically. Peptides also have fewer off-target effects. Small molecules are easy to administer, inexpensive to make and cross the blood-brain barrier more rapidly. For this reason, the team resorted to computational tools and artificial intelligence to come up with a new small molecular drug based on these peptides. This can be taken orally, and is similar in size and structure to the medications used for medical conditions like high blood pressure. An optimized version is being developed to enable human trials to be conducted. The work so far has taken about two decades, building step upon painstaking step to come up with the right solution. However, says Jhamandas, “Occasionally you come across a discovery that has the potential to change the game in a very fundamental way, like hitting a home run, and I'm very excited that we are really on to something here.” Short amylin receptor antagonist peptides improve memory deficits in Alzheimer’s disease mouse model. Rania Soudy, Ryoichi Kimura, Aarti Patel, Wen Fu, Kamaljit Kaur, David Westaway, Jing Yang & Jack Jhamandas. Scientific Reports, volume 9, Article number: 10942 (2019). https://doi.org/10.1038/s41598-019-47255-9. https://www.nature.com/articles/s41598-019-47255-9

Source: www.news-medical.net ↗
comparison

Comparisons

Side-by-side pages for commonly compared peptides and research compounds.

Source: peptideuniv.com
Research context

Read sources and limitations before applying a claim.

Longevity, Performance & Obesity Research

A research peptide formulation developed to investigate metabolic regulation, mitochondrial function, and nutrient-sensing pathways.

Source: mypeptidematch.com ↗
P

About the author

Peptide Therapy Guide Editorial Team

Editorial team for Peptide Therapy Guide.

View all articles →