Sh-Polypeptide-1 (EGF)

Sh-Polypeptide-1 is the INCI name for recombinant human epidermal growth factor (rh-EGF), a 53-amino acid polypeptide that plays a critical role in regulating cell growth, proliferation, and differentiation. EGF was first discovered by Dr. Stanley Cohen in 1962, a discovery that earned him the Nobel Prize in Physiology or Medicine in 1986. The recombinant form is produced through biotechnological processes using yeast, bacteria, or other expression systems.

EGF exerts its biological effects by binding to the epidermal growth factor receptor (EGFR), a transmembrane tyrosine kinase receptor found on the surface of epithelial cells, fibroblasts, and other cell types. This binding triggers a cascade of intracellular signaling events that promote cell division, migration, and the production of extracellular matrix components. In the context of skin, EGF stimulates keratinocyte and fibroblast proliferation, accelerates wound re-epithelialization, and enhances overall skin renewal.

In medical applications, recombinant EGF has been studied extensively for wound healing, particularly diabetic foot ulcers and burn injuries. The product Heberprot-P, developed in Cuba, uses recombinant EGF injected directly into diabetic foot ulcers, demonstrating significant improvements in healing rates and reduction in amputations. In South Korea, topical EGF formulations have been approved for wound healing applications.

In the cosmetic industry, Sh-Polypeptide-1 is used in anti-aging products targeting skin renewal and regeneration. By promoting cell turnover, EGF-containing products aim to improve skin texture, reduce fine lines, and enhance overall skin radiance. However, there is ongoing scientific debate about whether topically applied EGF can effectively penetrate the skin barrier in sufficient quantities to produce meaningful biological effects in intact skin.