A new decorin‐like tetrapeptide for optimal organization of collagen fibers

Abstract

Citation: IFSCC Magazine, 10 (2007) (4) 309–314Decorin interacts with collagen via its protein core and influences collagen fibrillogenesis, thus regulating excessive bundle‐like aggregation of collagen. As skin ages, there is a lack of functional decorin which results in disrupted collagen fibers and a reduction in the tensile strength of the skin. Therefore, a substitute for decorin would make up for the non‐functional decorin that is present as we age.Two tetrapeptide sequences were identified as the specific binding sites of decorin to collagen fibrils. These sequences were engineered in order to generate new tetrapeptides with improved affinity that would present a decorin‐like activity. A focused library of several candidates was synthesized containing only tetrapeptides that mimicked the binding sequences of decorin. The candidates were screened with an in vitro collagen fibrillogenesis assay, and the tetrapeptide with the INCI name Tripeptide‐10 Citrulline achieved the best results. Like decorin, this synthetic tetrapeptide proved in in vitro tests to regulate collagen fibrillogenesis and influence the diameter of collagen fibers, making them thinner and more uniform. Tripeptide‐10 citrulline is a new cosmetic active to specifically target collagen fiber organization. Skin collagen quality is addressed rather than skin collagen quantity. Tripeptide‐10 citrulline ensures uniformity of fibril diameter and increases skin suppleness due to a better cohesion of collagen fibers.Keywords: collagen, decorin, diameter, fiber, organizationWinner of the Award for the best Podium Presentation at the IFSCC Conference 2007, Amsterdam, The Netherlands