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Collagen supplementation: The Key for Post-workout Recovery and Healthy Ageing

-Disclaimer: The purpose of this article is solely to provide information; it does not prescribe or recommend intake. Any supplementation or diet should always be consulted with your registered dietician or GP-

Author: Irene Molina-Gonzalez, PhD

As part of my MSc in Sports and Exercise Science and Medicine, I recently wrote an article on an ergogenic aid. I decided to focus on collagen supplementation because it is a fascinating protein that can aid in recovery after intense workouts and potentially assist with healthy joint ageing, which is particularly important for women. I'll explain why in this article!

Collagens are a type of protein that is found abundantly in the human body. They make up a significant portion of the extracellular matrix, which is the area between cells. Proteins in the extracellular matrix play a vital role in controlling the function of cells in our tissues. Collagens provide stability to our tissues and protect them from being overstretched.

Various types of collagens are present in our body, such as skin, bones, cartilage, tendons and muscles. However, this article will discuss on the collagens found in our joints, muscles and bones. Additionally, I will briefly summarise the content of my previous article on the strength gains achieved through exercise with collagen supplementation.

Collagen synthesis after exercise and collagen supplementation

Regular exercise stimulates natural collagen production. This is extremely beneficial as it helps build strength and makes tissues more resilient and capable of handling more intense training and weight. This adaptation is crucial as collagen strengthens our tissues and prevents them from injuries. Studies conducted on humans have investigated the production of collagen after exercise. They have found that both men and women experience a rapid increase in collagen synthesis levels in muscle and tendons, peaking after 2-3 days post-exercise [1, 2]. Interestingly, collagen levels remain high for up to a month after exercise [3], indicating that these gains in support and rigidity in our tissues are long-lasting.

Collagen is extracted from gelatine derived from animals' rich-collagen tissue. Collagen supplements are taken in the form of peptides. This means collagen is broken down into smaller pieces to make it easier to absorb [4]. When we take collagen supplements, human studies have shown that the amino acids in collagen increase in our blood after 1-2 hours [5, 6]. Studies conducted in rodents have also demonstrated that collagen is quickly taken up by the tissues in our body, such as cartilage, bones, and muscles [7].

When fortified with essential amino acids, collagen can be just as efficient as whey in building muscle strength [8]. Collagen supplements usually contain Vitamin C, which boosts collagen production [9]. Significantly, it can aid in recovery and alleviate joint pain following intense exercise. In a study, highly active young adults were given collagen peptides for 12 weeks [10]. The study found that the participants experienced improved pain levels compared to the control group [10]. Similarly, in a large study done in physically active individuals, daily collagen supplementation for 24 weeks resulted in arthralgia reduction after intense exercise [11].

Collagen in ageing and injury

As tissues age, they become more fragile and less resistant to stress and strain. In aged populations, collagen, along with exercise, can help prevent these changes. Studies have shown that supplementing with collagen can increase muscle strength, and bone mass more than exercise alone, especially when fortified with leucine [12]. Moreover, a randomised trial conducted by Mertz and colleagues (2021) showed that in participants over the age of 65, the efficacy of protein supplementation was apparent only when paired with resistance training, as opposed to when it was administered alone [13]. High weightlifting exercise has proved to be more effective in promoting muscle gains [13].

As we age, our protein consumption often decreases, and our diets become hipoenergetic. Additionally, reduced physical activity can lead to significant muscle mass loss, increasing the risk of developing sarcopenia. Muscle loss can also occur due to illness or injury. When we are hospitalised, our energy intake is often inadequate, and physical activity is limited. Research suggests that collagen supplementation may help maintain muscle mass in these scenarios [14, 15].

Collagen for osteoporosis and osteoarthritis

Collagen can help reduce pain in individuals with osteoarthritis and osteoporosis by increasing bone mineral density, protecting cartilage from damage, and reducing perceived pain [16, 17]. This may be especially relevant to women as they have a higher incidence of these diseases. Oestrogen may regulate collagen levels. A hallmark for osteoporosis has been linked to oestrogen deficiency as in menopause [18], whereas only a small correlation has been found for osteoarthritis [19]. Interestingly, women at rest have lower levels of collagen synthesis in tendons than men [1]. Therefore, some other unknown sex-related mechanisms may also regulate this difference.

A study showed that consuming supplements containing collagen II (a type of collagen found in cartilage) was beneficial in reducing joint pain caused by physical activity in healthy individuals aged 46 years or above [20]. In this study, participants underwent pain-inducing exercises for 4-months. Those who took collagen supplements experienced lesser pain during and after exercise and also improved the range of motion in their knees as compared to the beginning of the study and a group that received a placebo (a drink with a similar taste, but without collagen) [20].

A six-month double-blinded randomised trial showed that patients with knee osteoarthritis experienced improvements in pain levels starting from week 13 after collagen supplementation [21]. Interestingly, the collagen used in this study was derived from bovine bone and pork skin, which mainly contains type I collagen. This suggests that the specific collagen type may not be as important for producing positive effects. Of note, these studies have important implications for the treatment and management of osteoarthritis.


Collagen is a crucial protein in connective tissue that provides support and resistance to breakdown. When taken as a supplement, the body quickly absorbs it and is transported to the required tissues. Collagen supplementation may help gain muscle after exercise and reduce joint pain after intense activities. It helps prevent muscle mass loss due to inactivity and can aid in preserving muscle strength if combined with resistance training during ageing and injury. Additionally, collagen has been suggested as a treatment for conditions like osteoporosis and osteoarthritis, where it plays an important role in maintaining bone strength and joint health. This may be especially relevant to women since oestrogen may regulate collagen levels, which decrease during menopause, increasing the risk of developing these diseases.

Yet, there are questions that still need to be answered;

Different studies use different doses, prompting the need for dose standardisation or potential personalisation. Should collagen intake differ between young and elderly individuals? Is early-life collagen supplementation advisable to prevent conditions like osteoarthritis and osteoporosis, especially in women? Additionally, should athletes consider collagen supplementation to aid with recovery, particularly in the context of injuries?


1.            Miller, B.F., et al., Tendon collagen synthesis at rest and after exercise in women. Journal of Applied Physiology, 2007. 102(2): p. 541-546.

2.            Miller, B.F., et al., Coordinated collagen and muscle protein synthesis in human patella tendon and quadriceps muscle after exercise. J Physiol, 2005. 567(Pt 3): p. 1021-33.

3.            Mendias, C.L., et al., Changes in muscle fiber contractility and extracellular matrix production during skeletal muscle hypertrophy. Journal of Applied Physiology, 2017. 122(3): p. 571-579.

4.            Figueres Juher, T. and E. Basés Pérez, [An overview of the beneficial effects of hydrolysed collagen intake on joint and bone health and on skin ageing]. Nutr Hosp, 2015. 32 Suppl 1: p. 62-6.

5.            Iwai, K., et al., Identification of Food-Derived Collagen Peptides in Human Blood after Oral Ingestion of Gelatin Hydrolysates. Journal of Agricultural and Food Chemistry, 2005. 53(16): p. 6531-6536.

6.            Oertzen-Hagemann, V., et al., Effects of 12 Weeks of Hypertrophy Resistance Exercise Training Combined with Collagen Peptide Supplementation on the Skeletal Muscle Proteome in Recreationally Active Men. Nutrients, 2019. 11(5): p. 1072.

7.            Oesser, S., et al., Oral Administration of 14C Labeled Gelatin Hydrolysate Leads to an Accumulation of Radioactivity in Cartilage of Mice (C57/BL). The Journal of Nutrition, 1999. 129(10): p. 1891-1895.

8.            Oikawa, S.Y., et al., Whey protein but not collagen peptides stimulate acute and longer-term muscle protein synthesis with and without resistance exercise in healthy older women: a randomized controlled trial. Am J Clin Nutr, 2020. 111(3): p. 708-718.

9.            Shaw, G., et al., Vitamin C–enriched gelatin supplementation before intermittent activity augments collagen synthesis12. The American Journal of Clinical Nutrition, 2017. 105(1): p. 136-143.

10.          Zdzieblik, D., et al., Improvement of activity-related knee joint discomfort following supplementation of specific collagen peptides. Applied Physiology, Nutrition, and Metabolism, 2017. 42(6): p. 588-595.

11.          Clark, K.L., et al., 24-Week study on the use of collagen hydrolysate as a dietary supplement in athletes with activity-related joint pain. Current Medical Research and Opinion, 2008. 24(5): p. 1485-1496.

12.          Zdzieblik, D., et al., Collagen peptide supplementation in combination with resistance training improves body composition and increases muscle strength in elderly sarcopenic men: a randomised controlled trial. Br J Nutr, 2015. 114(8): p. 1237-45.

13.          Mertz, K.H., et al., The effect of daily protein supplementation, with or without resistance training for 1 year, on muscle size, strength, and function in healthy older adults: A randomized controlled trial. The American Journal of Clinical Nutrition, 2021. 113(4): p. 790-800.

14.          Oikawa, S.Y., et al., A randomized controlled trial of the impact of protein supplementation on leg lean mass and integrated muscle protein synthesis during inactivity and energy restriction in older persons. The American Journal of Clinical Nutrition, 2018. 108(5): p. 1060-1068.

15.          Hays, N.P., et al., Effects of whey and fortified collagen hydrolysate protein supplements on nitrogen balance and body composition in older women. J Am Diet Assoc, 2009. 109(6): p. 1082-7.

16.          Porfírio, E. and G.B. Fanaro, Collagen supplementation as a complementary therapy for the prevention and treatment of osteoporosis and osteoarthritis: a systematic review. Revista Brasileira de Geriatria e Gerontologia, 2016. 19.

17.          Bello, A.E. and S. Oesser, Collagen hydrolysate for the treatment of osteoarthritis and other joint disorders: a review of the literature. Curr Med Res Opin, 2006. 22(11): p. 2221-32.

18.          Raisz, L.G., Pathogenesis of osteoporosis: concepts, conflicts, and prospects. J Clin Invest, 2005. 115(12): p. 3318-25.

19.          Bay-Jensen, A.C., et al., The response to oestrogen deprivation of the cartilage collagen degradation marker, CTX-II, is unique compared with other markers of collagen turnover. Arthritis Res Ther, 2009. 11(1): p. R9.

20.          Lugo, J.P., et al., Undenatured type II collagen (UC-II®) for joint support: a randomized, double-blind, placebo-controlled study in healthy volunteers. Journal of the International Society of Sports Nutrition, 2013. 10(1): p. 48.

21.          Kumar, V., et al., Human muscle protein synthesis and breakdown during and after exercise. J Appl Physiol (1985), 2009. 106(6): p. 2026-39.


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