Longevity PapersAbout
← All papers
RESEARCH PAPER / 2025-06-22

27P silk bioactive peptides mediate multifaceted regulation of collagen and support balance in fibroblast subpopulations.

SaiLavanyaa Sundar, Marios Frantzeskos Sardis, Lior Artzi, Aneesha Polisety, Setu Vora, Greg Altman, Svetlana Marukian

Evolved by Nature, Needham, Massachusetts, USA. Electronic address: [email protected]. · pubmed

Abstract

Fibroblasts play a key role in maintaining skin structure and immune balance, but factors like aging, stress, and chronic inflammation can weaken their function, leading to collagen loss, thinning skin, and increased inflammation. Traditional collagen boosters like retinoic acid (RA), vitamin C (VC), hyaluronic acid (HA), and transforming growth factor beta (TGFβ) have drawbacks, including poor absorption, instability, and irritation. Studies reveal that Silk Bioactive Peptide (27 P peptide) binds to epidermis and dermal fibroblasts, enhancing prolonged pro-collagen 1 (pro-C1) secretion in 3D and 2D models. De-novo collagen synthesis by 27 P peptide, likely regulated at the translational level, resulted in elevated collagen deposition and matrix remodeling up to 120 h. Combination of VC and 27 P peptide rescues VC-induced intracellular collagen depletion. Unlike TGFβ and RA, 27 P peptide maintains balance between fibroblast subpopulations, without inducing markers of fibrosis or inflammation. Together, 27 P peptide presents as a promising alternative to effectively promote collagen production, fibroblast homeostasis and skin health.

The following analysis is generated by AI and may contain errors. It is separate from the authors’ abstract and is not peer review.

Research summary

The paper claims that 27P silk bioactive peptides enhance collagen production and maintain fibroblast homeostasis without inducing fibrosis or inflammation. This research is relevant as it addresses mechanisms that could potentially mitigate age-related skin degeneration and promote healthier aging by targeting fibroblast function and collagen synthesis.

Author of this paper? Send a correction.