Clinical Studies on CYNERGY MEDTM Collagen

CYNERGY MEDTM is a Food Supplement with a naturally bioactive hydrolyzed collagen enhanced with hyaluronic acid and vitamins.

Clinical studies in Europe and Worldwide by World renowned Laboratories confirm that CYNERGY MEDTM is a product of excellent efficacy and emphasize its benefits.


 Clinical studies have shown that successful improvement of skin quality and structure can be achieved within 12 weeks of consumption.

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The dermis (substrate) skin where collagen peptides have acted in order to produce structuring substances for the formation of elastine and have aroused the multiplication of fibroblasts and collagen and Hyaluronic acid synthesis.

Moreover, the same hydrolysis process plays an important role in the quality of amino acids that are provided by the product. Hydrolysis with a method used for the production of PEPTAN™ guarantees that the ingredients are delivered to the body intact according to the procedural methods that are set by the strict production quality criteria for each production batch from the date of production until the date of consumption.

Source: Peptan, Rousselot Beauty Brochure, 2013 clinical studies results

CYNERGY MED™ Collagen is a nutricosmetic and dietary skin supplement. Clinical studies prove the significant benefits of its ingredients which in the formula found in CYNERGY MED™ Collagen bring about ultimate analogies of micronutritional elements for the nourishment, revitalization and inner correction of the skin.
Clinical Studies* on PEPTAN™ fish collagen have shown that with 12 weeks of use the improvement of skin state and structure is achieved.

Hydration results (Study YNTKK – 2008-4144)


Anti-aging results (Study 2008-?00654-51)

clinical-studies-beauty-01 Deep wrinkles graph clinical-studies-beauty-01

*Beauty Clinical Studies: References

  1. Nutricosmetics: a global strategic business report, Global Industry Analysts Inc, 2011
  2. Gniadecka M, Nielsen OF, Wessel S, Heidenheim M, Christensen DH, Wulf HC, 1998. Water and protein structure in photoaged and chronically aged skin. J Invest Dermatol 111 (6): 1129-1133
  3. Varani J, Dame MK, Rittie L, Fligiel S, Kang S, Fisher G, Voorhees JJ, 2006. Decreased collagen production in chronologically aged skin, Am J Pathol 168 (6): 1861-1868
  4. Clinical study, Cosderma, France, 2012
  5. Clinical study YNTKK – 2008 – 4144, Souken, Japan.
  6. Clinical study 2008 – AOO654 – 51, Dermscan, France
  7. Postlethwaite AE, Seyer JM, Kang AH, 1978. Chemotactic attraction of human fibroblasts to type I, II, and II collagens and collagen-derived peptides. Proc Nat Acad Sci USA 75 (2): 871-875
  8. Shigemura Y, Iwai K, Morimatsu F, Iwamoto T, Mori, Oda C, Taira T, Park Ey Nakamura Y, Sato K, 2009. Effect of prolyl-hydroxyproline (Pro-Hyp), a food-derived collagen peptide in human blood, on growth of fibroblasts from mouse skin. J Agric Food Chem 57 (2): 444-449
  9. Ohara H, Ichikawa S, Matsumoto H, Akiyama M, Fujimoto N, Kobayashi T, Tajima S, 2010. Collagen-derived dipeptide, proline-hydroxyproline, stimulates cell proliferation and hyaluronic acid synthesis in cultured human dermal fibroblasts. J Dermatol 374: 330-338
  10. Matsuda N, Koyama Y, Hosaka Y, Ueda H, Watanabe T, Araya S, Irie S, Takehana K, 2006. Effects of ingestion of collagen peptide on collagen fibrils and glycosaminoglycans in the dermis. J Nutr Sci Vitaminol 52: 211-215
  11. Matsumoto H, Ohara H, Ito K, Nakamura Y, Takahashi S, 2006. Clinical effects of fish type I collagen hydrolysate on skin properties. ITE Letters on Batteries, New Technologies and Medicine, 7 (4): 3 86-390
  12. Sumida E, Hirota A, Kuwaba K, Kusubata M, Koyama Y, Araya T, Irie S, Kasugai S, 2004. The effect of oral ingestion of collagen peptide on skin hydration and biochemical data of blood. J Nutritional Food 7 (3): 45-52
  13. Morganti P, Randazzo SD, Bruno C, 1988. Oral treatment of skin dryness. Cosmetics and Toiletries 103: 77-80
  14. Ichikawa S, Morifuji M, Ohara H, Matsumoto H, Takeuchi Y, Sato K, 2010. Hydroxyproline-containing dipeptides and tripeptides quantified at high concentration in human blood after oral administration of gelatine hydrolysate. Inter J Food Sci Nutr 61 (1): 52-60
  15. Watanabe-Kamiyama M, Shimizu M, Kamiyama S, Taguchi Y, Sone H, Morimatsu F, Shirakawa H, Furukawa Y, Komai M, 2010. Absorption and effectiveness of orally administered low molecular weight collagen hydrolysate in rats. J Agric Food Chem 58 (2): 835-841

Bones and Joints

Regarding bones, Peptan® has been shown to:

  • Restore bone mineral density.
  • Increase bone size, making them less brittle.
  • Stimulate osteoblast activity in spite of osteoclasts activity; the growth of the bone is stimulated.

Regarding joints, collagen peptides have been shown to:

  • Restore bone mineral density.
  • Orally taken collagen peptides are accumulated in cartilage as soon as 12 hours after the ingestion and the cells of the joint, the chondrocytes, respond to external collagen by producing a dose-dependant production of internal collagen.

Positive Effect of Peptan® on joint cells

Results of Peptan® study confirm the positive effect of Peptan® collagen peptides on joint cells (chondrocytes).
A dose of 10g of collagen peptides per day has demonstrated a positive effect on joint pain reduction. The integrity of articular cartilage is dependent on the maintenance of the extracellular matrix, a process controlled by the joint cells, the chondrocytes. The objective of the present study with a cell culture model was to investigate the effect of Peptan® collagen on the main components of the extracellular matrix of the cartilage: aggrecan and type II collagen.


The mechanism of action of collagen peptides


Positive Effect of Peptan® on cartillage

Cartilage consists of a single cell type, chondrocytes embedded in extracellular matrix made up of two major components: type II collagen which imparts tensile strength to the tissue and aggrecan that provides the ability of cartilage to resist compressive force. Orchestrated synthesis and turnover ensures and maintains the biochemical characteristic of the cartilage.


Peptan® B at 0.1 or 1 mg/mL concentrations over 8 days significantly enhanced the expression of aggrecan and type II collagen mRNA. These results demonstrate that Peptan® specifically enhanced the chondrocyte gene expression of the cartilage extra cellular matrix components.

Effect of Peptan® collagen peptides on knee joint pain and joint function in women with knee osteoarthritis

Osteoarthritis is one of the major causes of disability in the developed world. Today, 10% of all men and 20% of all women over 60 years old suffer from the disease. The prevalence of osteoarthritis will rise even further in the coming years linked to the increasingly aged population worldwide.
Joint pain, stiffness and locking are key symptoms of osteoarthritis causing impaired mobility and decreasing the quality of life of the patient. Only symptomatic treatments like pain killers and anti-inflammatory drugs are available which may cause heavy side effects. The final treatment is joint replacement by surgery.

Comprehensive studies have already shown Peptan® bioavailability and benefits on joint health.


Effect of Peptan® Collagen peptides on bones

Hydrolyzed collagen is useful in treating osteoporosis. In studies carried out, an increase in bone density was noticed in comparison to a control group. In studies carried out and published in “Bone Journal”, the effects of Peptan® in bone metabolism were confirmed and its mechanisms of action highlighted. In response to consumer concerns about bone health in the long run, various studies have been carried out – for quite a few years – showing that the oral administration of Peptan® has positive effects in osteopenia. Researchers who have conducted in vitro studies have emphasized that the cultivation of bone cells with Peptan® induced a clear differentiation of osteoblasts. These positive results have been confirmed in test in vivo. The researchers concluded that Peptan® can give back bone density by stimulating the growth and differentiation of osteoblasts, something particularly interesting in order to prevent the reduction of bone mass density with age*.

The measures show restoration of the bone mineral density value close to the level of the control group (which was not ovariectomized).

Peptan® restores bone mineral density

Peptan® increases bone size and solidity

Effect of Peptan® Collagen peptides on muscles

Loss of muscle mass – Sarcopenia

Sarcopenia (from Greek meaning “poverty of flesh”) is the degenerative loss of skeletal muscle mass and strength associated with aging : 0.5-1% loss per year after the age of 25!

This loss of muscle mass may be caused by different cellular mechanisms than those causing muscle atrophy. For example, during sarcopenia, there is a replacement of muscle fibers with fat and an increase in fibrosis.

Advantage of Collagen peptides over whey hydrolysate for Nitrogen balance

During a 15-day diet trial on 9 elderly women consumed whey or tryptophan fortified collagen peptides supplements. The supplements constituted about half of the total protein provided.

*Bones and Joints References

  1. Nomura, Y., Oohashi, K., Watanabe, M. and Kasugai, S. 2005. Increase in bone mineral density through oral administration of shark gelatine to ovariectomized rats. Nutrition, 21: 1120-1126.
  2. Wu, J., Fujioka, M., Sugimoto, K., Mu, G. and Ishimi, Y. 2004. Assessment of effectiveness of oral administration of collagen peptide on bone metabolism in growing and mature rats. Journal of bone and mineral metabolism, 22: 547-553.
  3. Karaguzel, G., Holick, M. 2010. Diagnosis and treatment of osteopenia. Rev Endocr Metab Disord, 11: 237-251.
  4. Mizuno, M. and Kuboki, Y. 2001. Osteoblast-related gene expression of bone marrow cells during the osteoblastic differentiation induced by type I collagen. Journal of biochemistry, 129: 133-138.
  5. Andrianarivo, A.G., Robinson, J.A., Mann, K.G. and Tracy R.P. 1992. Growth on type I collagen promotes expression of the osteoblastic phenotype in human osteosarcoma MG-63 cells. Journal of cellular physiology, 153: 256-265.
  6. Lynch, M.P., Stein, J.L., Stein, G.S. and Lian, J.B. 1995. The influence of type I collagen on the development and maintenance of the osteoblast phenotype in primary and passaged rat calvarial osteoblasts: modification of expression of genes supporting cell growth, adhesion, and extracellular matrix mineralization. Experimental cell research, 216: 35-45.
  7. Guillerminet, F., Beaupied, H., Fabien-Soul?, V., Tom?, D., Benhamou, C-L., Blachier, F., Roux, C. and Blais, A. 2010. collagen peptides improves bone metabolism and biomechanical parameters in ovariectomized mice: an in vitro and in vivo study. Bone.
  8. Moskowitz, R. 2000. Role of collagen hydrolysate in bone and joint disease. Seminars in arthritis and rheumatism, 30 (2): 87-99.
  9. Ruiz-Benito, P., Camacho-Zambrano, M.M., Carrillo-Arcentales, J.N., Mestanza-Peralta, M.A., Vallejo-Flores, C.A., Vargas-Lopez, S.V., Villacis-Tamayo, R.A. and Zurita-Gavilanes, L.A. 2009. A randomized controlled trial on the efficacy and safety of a food ingredient, collagen hydrolysate, for improving joint comfort. International journal of food sciences and nutrition, 12:1-15.
  10. Clark, K.L., Sebastianelli, W., Flechsenhar, K.R., Aukermann, D.F., Meza, F., Millard, R.L., Deitch, J.R., Sherbondy, P.S. and Albert, A.. 2008. 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, 24 (5): 1485-1496.
  11. Oesser, S., Adam, M., Babel, W. and Seifert, J. 1999. Oral administration of 14C labelled gelatine hydrolysate leads to an accumulation of radioactivity in cartilage of mice (C57/BL). Journal of nutrition, 129: 1891-1895.
  12. Oesser, S. and Seifert, J. 2003. Stimulation of type II collagen biosynthesis and secretion in bovine chondrocytes cultured with degraded collagen. Cell tissue research, 311: 393-399.
  13. Pasco, J.A, Seeman, E., Henry M.J, Merriman, E.N, Nicholson, G.C, Kotowicz, M.A. 2006. The population burden of fractures originates in women with osteopenia, not osteoporosis. Osteoporosis Int, 17: 1404-1409.
  14. Kiani C, Chen L., Wu Y.J., Yee J. A., Yang B.B. Structure and function of aggrecan. Cell Research 2002; 12(1):19-32.
  15. Sofat N. Analysing the role of endogenous matrix molecules in the development of osteoarthritis. Int J Exp Pathol. 2009 Oct; 90(5): 463-79.
  16. Schulze-Tanzil G. Activation and dedifferentiation of chondrocytes: implications in cartilage injury and repair. Ann Anat. 2009 Oct; 191(4): 325-38.
  17. http://www.who.int/chp/topics/rheumatic/en/
  18. Ichikawa S, Morifuji M, Ohara H, Matsumoto H, Takeuchi Y, Sato K (2010). Hydroxyproline-containing dipeptides and tripeptides quantified at high concentration in human blood after oral administration of gelatine hydrolysate. International Journal of Food Sciences and Nutrition 61(1):52-60.
  19. Schunck M, Schulze CH, Oesser S (2007). Collagen hydrolysate supplementation stimulates proteoglycan metabolism and gene expression of articular chondrocytes. International Cartilage Repair Society Poster #189.
  20. Ohara H, Ichikawa S, Matsumoto H, Akiyama M, Fujimoto N, Kobayashi T, Tajima S (2010) Collagen-derived dipeptide, proline-hydroxyproline, stimulates cell proliferation and hyaluronic acid synthesis in cultured human dermal fibroblasts. Journal of Dermatology 37(4): 330-338.
  21. Trc T, Bohmova J (2011). Efficacy and tolerance of enzymatic hydrolysed collagen (EHC) vs. glucosamine sulphate (GS) in the treatment of knee osteoarthritis (KOA). International Orthopaedics 35(3):341–348.
  22. Bruyere O, Zegels B, Leonori L, Rabenda V, Janssen A, Bourges C, Reginster JY (2012). Effect of collagen hydrolysate in articular pain: A 6-month randomized, double-blind, placebo controlled study. Complementary Therapies in Medicine 20(3):124-30.
  23. Bellamy N, Buchanan WW, Goldsmith CH, Campbell J, Stitt LW (1988). Validation study of WOMAC: a health status instrument for measuring clinically important patient relevant outcomes to antirheumatic drug therapy in patients with osteoarthritis of the hip or knee. Journal of Rheumatology 15(12):1833-40.
  24. Lysholm J, Gillquist J (1982). Evaluation of knee ligament surgery results with special emphasis on use of a scoring scale. American Journal of Sports Medicine 10(3):150-4.


Laboratory’s in vitro digestibility results

The test has been based on the Glahn’s method and consists of the following successive steps which mimic the real digestion:

  • Oral step = mechanical food breaking and salivary enzyme action
  • Gastric step = acidic pH and addition of gastric enzymes
  • Intestinal step = pH near from the neutrality, addition of pancreatic enzymes and biliary salt actions
  • At the end of the digestion, the samples are analysed by high performance size exclusion chromatography (HPSEC) i.e. particles are separated depending on their sizes

PeptanTM digestibility

After the in vitro digestion process, around 90 % of the Peptan™ have been digested in peptides whose molecular weight is below 2000 Dalton and which can be absorbed by the intestine.


Those profiles confirm that the molecular weight decreased after digestion. 90% of the Peptan™ derived peptides are below 2000 Dalton.
Those results are fully in line with literature.


Literature has shown from recent studies that:

  • Collagen Peptides are fully digested by the intestinal track in small peptides.
  • Those peptides are then well absorbed and transported by the blood stream to the skin in order to come in contact with fibroblasts in the dermis.

Laboratory’s results

  • Laboratory results have demonstrated through in vitro studies that Peptan Collagen Peptides are fully digested by the intestine and can be well absorbed.