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Tripeptide-10 Citrulline, a substitute of decorin
An overview of Tripeptide-10 Citrulline
Signal oligopeptides are commonly synthesized from portions of EMPs and from natural peptides in the environment that mimic these structural macromolecules. Signal oligopeptides, also known as matrikines, stimulate dermal fibroblasts to proliferate and alter their protein expression patterns. Tripeptide-10 Citrulline is a short peptide segment of decorin, the most common GAG in wound healing sites.
Decorin is a leucine-rich proteoglycan commonly found amongst ECPs. Its role is to stabilize the organization of collagen fibrils into longer, thicker cables, that help support the extracellular scaffold of the epidermis. A horeshoe-shaped molecule, decorin binds two triple helix collagen fibrils and orients them in a staggered manner to increase collagen fiber growth and maintain tissue shape. Tripeptide-10 Citrulline, or Decorinyl, is a tetrapeptide engineered in 2008 from decorin, whose peptide chain follows the +, -, 0, +charge pattern, indicating that the binding of decorin to collagen is required.
Tripeptide-10 citrulline not only helps regulate fiber production, but also regulates the size and uniformity of collagen fibers, making this oligopeptide a good candidate for skin elasticity and wrinkle reduction.
The study and function of Tripeptide-10 Citrulline
A single-blinded parallel group controll trial compared cream containing Tripeptide-10 Citrulline to placebo. After 28 days, results showed an increase of skin suppleness by 54%, an effect seen in 95% of volunteers. In conclusion, Tripeptide-10 (aspartic acid with isoleucine and lysine) is used as a firming agent because it has a good candidate effect of maintaining skin elasticity and reducing wrinkles.
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4. Raikou, V., Varvaresou, A., Panderi, I., & Papageorgiou, E. (2017). The efficacy study of the combination of tripeptide-10-citrulline and acetyl hexapeptide-3. A prospective, randomized controlled study. Journal of cosmetic dermatology, 16 (2), 271-278.