Hexapeptide-10 / Serilesine

Hexapeptide-10, marketed as Serilesine®, is a synthetic six-amino acid peptide (Ser-Ile-Lys-Val-Ala-Val) designed to replicate bioactive adhesion sequences found within laminin-5 — a critical structural glycoprotein of the dermal-epidermal junction (DEJ). The DEJ is the basement membrane zone that anchors the epidermis to the dermis through specialized adhesion complexes including hemidesmosomes, anchoring fibrils, and laminin-5 networks. With aging, UV exposure, and disease states, DEJ integrity weakens, resulting in loss of skin density, firmness, and structural cohesion. Upon topical application, Hexapeptide-10 binds α6β4 integrin receptors on keratinocytes, mimicking the cell-adhesion domain of laminin-5 and triggering downstream signaling that upregulates synthesis of laminin-5 itself, collagen XVII (BP180), and other hemidesmosomal components. Simultaneously, the peptide stimulates fibroblasts in the papillary dermis to produce laminin-1 and anchoring collagen VII, collectively strengthening DEJ architecture. In vitro studies show Hexapeptide-10 increases laminin-5 mRNA expression by over 100% and improves hemidesmosome density by approximately 35% in keratinocyte cultures. Research applications include skin restructuring, firmness improvement, anti-sagging, and wound healing investigations. Clinical studies report significant improvements in skin compactness, elasticity, and density with 1–2% Hexapeptide-10 formulations. The peptide's unique mechanism — targeting the DEJ rather than surface collagen — makes it particularly valuable for research into deep skin architecture and the structural basis of skin aging.