Complexe multi-collagène : peptides de collagène bovin hydrolysé nourris à l'herbe, bouillon d'os de bœuf biologique, bouillon d'os de poulet biologique, peptides de collagène de poisson hydrolysé sauvage, collagène membranaire de coquille d'œuf, café instantané Kona. Autres ingrédients : arôme de cacao, arôme naturel de vanille.

Profil d'acides aminés (milligrammes moyens par portion) : Alanine 867 mg, Arginine 737 mg, Acide aspartique 558 mg, Acide glutamique 979 mg, Glycine 2334 mg, Histidine 73 mg, Hydroxylysine 85 mg, Hydroxyproline 1134 mg, Isoleucine 149 mg, Leucine 285 mg, Lysine 358 mg, Méthionine 86 mg, Phénylalanine 189 mg, Proline 1354 mg, Sérine 325 mg, Thréonine 177 mg, Tyrosine 50 mg, Valine 220 mg. Milligrammes moyens par portion d'origine naturelle ; les valeurs absolues peuvent varier. Contient 8 des 9 acides aminés essentiels. Pas une source significative de protéines. La protéine de collagène ne compte pas dans le pourcentage de valeur quotidienne recommandée par la FDA pour les protéines, car il lui manque un acide aminé essentiel : le tryptophane. Emballé au poids et non au volume. Un tassement peut se produire.

Les adultes prennent 1 à 2 cuillères à soupe de Codeage Multi Collagen Peptides Mocha avec 8 à 12 onces d'eau ou votre boisson préférée ou selon les directives d'un professionnel de la santé qualifié.

ATTENTION : Ne dépassez pas la dose recommandée. NE PAS utiliser ce produit si vous avez des allergies ou des sensibilités aux œufs, au poisson ou à l'un des ingrédients répertoriés. En cas d'inconfort gastro-intestinal (y compris ballonnements, crampes, diarrhée ou autres troubles digestifs) ou d'autres sensibilités, ARRÊTEZ immédiatement de prendre le produit. Les mères enceintes ou allaitantes et les personnes souffrant d'un problème de santé connu doivent consulter un médecin avant d'utiliser ce produit ou tout autre complément alimentaire. Utilisez ce produit uniquement comme complément alimentaire. Ne pas utiliser pour la réduction de poids.

Kona Instant Coffee

Carlsen MH, Halvorsen BL, Holte K, et al. The total antioxidant content of more than 3100 foods, beverages, spices, herbs and supplements used worldwide. Nutr J. 2010;9:3. Published 2010 Jan 22. doi: 10.1186/1475-2891-9-3

Yashin A, Yashin Y, Wang JY, Nemzer B. Antioxidant and Antiradical Activity of Coffee. Antioxidants (Basel). 2013;2(4):230‐245. Published 2013 Oct 15. doi: 10.3390/antiox2040230

Fusco D, Colloca G, Lo Monaco MR, Cesari M. Effects of antioxidant supplementation on the aging process. Clin Interv Aging. 2007;2(3):377‐387. PMCID: PMC2685276

JI, L.L., LEEUWENBURGH, C., LEICHTWEIS, S., GORE, M., FIEBIG, R., HOLLANDER, J. and BEJMA, J. (1998), Oxidative Stress and Aging: Role of Exercise and Its Influences on Antioxidant Systems. Annals of the New York Academy of Sciences, 854: 102-117. DOI: 10.1111/j.1749-6632.1998.tb09896.x

De la Fuente, M. Effects of antioxidants on immune system ageing. Eur J Clin Nutr 56, S5–S8 (2002). DOI: 10.1038/sj.ejcn.1601476

Bonnefoy, M., Drai, J., & Kostka, T. (2002). [Antioxidants to slow aging, facts and perspectives]. Presse medicale, 31 25, 1174-84 .

JOYE K. WILLCOX, SARAH L. ASH & GEORGE L. CATIGNANI (2004) Antioxidants and Prevention of Chronic Disease, Critical Reviews in Food Science and Nutrition, 44:4, 275-295, DOI: 10.1080/10408690490468489

Grass-Fed Hydrolyzed Bovine Collagen Peptides

Vollmer DL, West VA, Lephart ED. Enhancing Skin Health: By Oral Administration of Natural Compounds and Minerals with Implications to the Dermal Microbiome. Int J Mol Sci. 2018;19(10):3059. Published 2018 Oct 7. doi: 10.3390/ijms19103059

Saha A, Alam MJ, Ashraf KU, Mannan A. Computational analysis of bovine alpha-1 collagen sequences. Bioinformation. 2013;9(1):42‐48. doi: 10.6026/97320630009042

León-López A, Morales-Peñaloza A, Martínez-Juárez VM, Vargas-Torres A, Zeugolis DI, Aguirre-Álvarez G. Hydrolyzed Collagen-Sources and Applications. Molecules. 2019;24(22):4031. Published 2019 Nov 7. doi: 10.3390/molecules24224031

K. Henriksen, M.A. Karsdal, in Biochemistry of Collagens, Laminins and Elastin, 2016

Albaugh VL, Mukherjee K, Barbul A. Proline Precursors and Collagen Synthesis: Biochemical Challenges of Nutrient Supplementation and Wound Healing. J Nutr. 2017;147(11):2011‐2017. doi:10.3945/jn.117.256404

Avila Rodríguez, MI, Rodríguez Barroso, LG, Sánchez, ML. Collagen: A review on its sources and potential cosmetic applications. J Cosmet. Dermatol. 2018; 17: 20– 26. DOI: 10.1111/jocd.12450

Paul C, Leser S, Oesser S. Significant Amounts of Functional Collagen Peptides Can Be Incorporated in the Diet While Maintaining Indispensable Amino Acid Balance. Nutrients. 2019;11(5):1079. Published 2019 May 15.  doi: 10.3945/jn.117.256404

Proksch, E., Segger, D., Degwert, J., Schunck, M., Zague, V., & Oesser, S. (2014). Oral supplementation of specific collagen peptides has beneficial effects on human skin physiology: a double-blind, placebo-controlled study. Skin pharmacology and physiology, 27(1), 47–55. DOI: 10.1159/000351376

Zdzieblik D, Oesser S, Baumstark MW, Gollhofer A, König D. 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):1237‐1245. doi: 10.1017/S0007114515002810

Organic Chicken Bone Broth

Crowley DC, Lau FC, Sharma P, et al. Safety and efficacy of undenatured type II collagen in the treatment of osteoarthritis of the knee: a clinical trial. Int J Med Sci. 2009;6(6):312‐321. Published 2009 Oct 9. doi: 10.7150/ijms.6.312

Bakilan F, Armagan O, Ozgen M, Tascioglu F, Bolluk O, Alatas O. Effects of Native Type II Collagen Treatment on Knee Osteoarthritis: A Randomized Controlled Trial. Eurasian J Med. 2016;48(2):95‐101. doi: 10.5152/eurasianjmed.2015.15030

Lugo, J.P., Saiyed, Z.M. & Lane, N.E. Efficacy and tolerability of an undenatured type II collagen supplement in modulating knee osteoarthritis symptoms: a multicenter randomized, double-blind, placebo-controlled study. Nutr J 15, 14 (2015). DOI: 10.1186/s12937-016-0130-8

Bagchi, D., Misner, B., Bagchi, M., Kothari, S. C., Downs, B. W., Fafard, R. D., & Preuss, H. G. (2002). Effects of orally administered undenatured type II collagen against arthritic inflammatory diseases: a mechanistic exploration. International journal of clinical pharmacology research, 22(3-4), 101–110.

Zhu, P., Li, X. Y., Wang, H. K., Jia, J. F., Zheng, Z. H., Ding, J., & Fan, C. M. (2007). Oral administration of type-II collagen peptide 250-270 suppresses specific cellular and humoral immune response in collagen-induced arthritis. Clinical immunology (Orlando, Fla.), 122(1), 75–84. DOI: 10.1016/j.clim.2006.08.004

Barnett, M. L., Kremer, J. M., St Clair, E. W., Clegg, D. O., Furst, D., Weisman, M., Fletcher, M. J., Chasan-Taber, S., Finger, E., Morales, A., Le, C. H., & Trentham, D. E. (1998). Treatment of rheumatoid arthritis with oral type II collagen. Results of a multicenter, double-blind, placebo-controlled trial. Arthritis and rheumatism, 41(2), 290–297. DOI: 10.1002/1529-0131(199802)41:2<290::AID-ART13>3.0.CO;2-R

Yoshinari, O., Moriyama, H., & Shiojima, Y. (2015). An overview of a novel, water-soluble undenatured type II collagen (NEXT-II). Journal of the American College of Nutrition, 34(3), 255–262. DOI: 10.1080/07315724.2014.919541

Paul, C., Leser, S., & Oesser, S. (2019). Significant Amounts of Functional Collagen Peptides Can Be Incorporated in the Diet While Maintaining Indispensable Amino Acid Balance. Nutrients, 11(5), 1079. DOI: 10.3390/nu11051079

Darling, A. L., Manders, R., Sahni, S., Zhu, K., Hewitt, C. E., Prince, R. L., Millward, D. J., & Lanham-New, S. A. (2019). Dietary protein and bone health across the life-course: an updated systematic review and meta-analysis over 40 years. Osteoporosis international : a journal established as result of cooperation between the European Foundation for Osteoporosis and the National Osteoporosis Foundation of the USA, 30(4), 741–761. DOI: 10.1007/s00198-019-04933-8

Lerman, R. H., Chang, J. L., Konda, V., Desai, A., & Montalto, M. B. (2015). Nutritional Approach for Relief of Joint Discomfort: A 12-week, Open-case Series and Illustrative Case Report. Integrative medicine (Encinitas, Calif.), 14(5), 52–61. PMCID: PMC4712866

Organic Beef Bone Broth

Di Lullo GA, Sweeney SM, Korkko J, Ala-Kokko L, San Antonio JD. Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen. The Journal of Biological Chemistry. 2002 Feb;277(6):4223-4231. DOI: 10.1074/jbc.M110709200

Xin Liu, Hong Wu, Michael Byrne, Stephen Krane, and Rudolf Jaenisch. Type III collagen is crucial for collagen I fibrillogenesis and for normal cardiovascular development. PNAS March 4, 1997 94 (5) 1852-1856. DOI: 10.1073/pnas.94.5.1852

Rebello, C. J., Liu, A. G., Greenway, F. L., & Dhurandhar, N. V. (2013). Dietary strategies to increase satiety. Advances in food and nutrition research, 69, 105–182. DOI: 10.1016/B978-0-12-410540-9.00003-X

Rubio, I. G., Castro, G., Zanini, A. C., & Medeiros-Neto, G. (2008). Oral ingestion of a hydrolyzed gelatin meal in subjects with normal weight and in obese patients: Postprandial effect on circulating gut peptides, glucose and... Eating and weight disorders : EWD, 13(1), 48–53. DOI: 10.1007/BF03327784

Veldhorst, M. A., Nieuwenhuizen, A. G., Hochstenbach-Waelen, A., Westerterp, K. R., Engelen, M. P., Brummer, R. J., Deutz, N. E., & Westerterp-Plantenga, M. S. (2009). A breakfast with alpha-lactalbumin, gelatin, or gelatin + TRP lowers energy intake at lunch compared with a breakfast with casein, soy, whey, or whey-GMP. Clinical nutrition (Edinburgh, Scotland), 28(2), 147–155. DOI: 10.1016/j.clnu.2008.12.003

Hochstenbach-Waelen, A., Westerterp-Plantenga, M. S., Veldhorst, M. A., & Westerterp, K. R. (2009). Single-protein casein and gelatin diets affect energy expenditure similarly but substrate balance and appetite differently in adults. The Journal of nutrition, 139(12), 2285–2292. DOI: 10.3945/jn.109.110403

Schunck, M., Zague, V., Oesser, S., & Proksch, E. (2015). Dietary Supplementation with Specific Collagen Peptides Has a Body Mass Index-Dependent Beneficial Effect on Cellulite Morphology. Journal of medicinal food, 18(12), 1340–1348. DOI: 10.1089/jmf.2015.0022

Wild Caught Hydrolyzed Fish Collagen

Sanchez A, Blanco M, Correa B, Perez-Martin RI, Sotelo CG. Effect of Fish Collagen Hydrolysates on Type I Collagen mRNA Levels of Human Dermal Fibroblast Culture. Mar Drugs. 2018;16(5):144. Published 2018 Apr 26. doi: 10.3390/md16050144

König D, Oesser S, Scharla S, Zdzieblik D, Gollhofer A. Specific Collagen Peptides Improve Bone Mineral Density and Bone Markers in Postmenopausal Women-A Randomized Controlled Study. Nutrients. 2018;10(1):97. Published 2018 Jan 16. doi: 10.3390/nu10010097

Porfírio, Elisângela & Fanaro, Gustavo. (2016). Collagen supplementation as a complementary therapy for the prevention and treatment of osteoporosis and osteoarthritis: a systematic review. Revista Brasileira de Geriatria e Gerontologia. 19. 153-164. DOI: 10.1590/1809-9823.2016.14145

De Luca C, Mikhal'chik EV, Suprun MV, Papacharalambous M, Truhanov AI, Korkina LG. Skin Antiageing and Systemic Redox Effects of Supplementation with Marine Collagen Peptides and Plant-Derived Antioxidants: A Single-Blind Case-Control Clinical Study. Oxid Med Cell Longev. 2016;2016:4389410. doi: 10.1155/2016/4389410

Glynis A. A Double-blind, Placebo-controlled Study Evaluating the Efficacy of an Oral Supplement in Women with Self-perceived Thinning Hair. J Clin Aesthet Dermatol. 2012;5(11):28‐34. PMCID: PMC3509882

Proksch, E., Schunck, M., Zague, V., Segger, D., Degwert, J., & Oesser, S. (2014). Oral intake of specific bioactive collagen peptides reduces skin wrinkles and increases dermal matrix synthesis. Skin pharmacology and physiology, 27(3), 113–119. DOI: 10.1159/000355523

Proksch, E., Segger, D., Degwert, J., Schunck, M., Zague, V., & Oesser, S. (2014). Oral supplementation of specific collagen peptides has beneficial effects on human skin physiology: a double-blind, placebo-controlled study. Skin pharmacology and physiology, 27(1), 47–55. DOI: 10.1159/000351376