CopA3 peptide prevents ultraviolet-induced inhibition of type-I procollagen and induction of matrix metalloproteinase-1 in human skin fibroblasts

Molecules. 2014 May 20;19(5):6407-14. doi: 10.3390/molecules19056407.

Abstract

Ultraviolet (UV) exposure is well-known to induce premature aging, which is mediated by matrix metalloproteinase-1 (MMP-1) activity. A 9-mer peptide, CopA3 (CopA3) was synthesized from a natural peptide, coprisin, which is isolated from the dung beetle Copris tripartitus. As part of our continuing search for novel bioactive natural products, CopA3 was investigated for its in vitro anti-skin photoaging activity. UV-induced inhibition of type-I procollagen and induction of MMP-1 were partially prevented in human skin fibroblasts by CopA3 peptide in a dose-dependent manner. At a concentration of 25 μM, CopA3 nearly completely inhibited MMP-1 expression. These results suggest that CopA3, an insect peptide, is a potential candidate for the prevention and treatment of skin aging.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antimicrobial Cationic Peptides / pharmacology*
  • Cells, Cultured
  • Collagen Type I / antagonists & inhibitors*
  • Collagen Type I / radiation effects
  • Dose-Response Relationship, Drug
  • Fibroblasts / drug effects*
  • Fibroblasts / metabolism*
  • Fibroblasts / radiation effects*
  • Insect Proteins / pharmacology*
  • Matrix Metalloproteinase 1 / genetics
  • Matrix Metalloproteinase 1 / metabolism*
  • Skin / cytology
  • Skin / metabolism
  • Skin / radiation effects
  • Skin Aging / drug effects
  • Ultraviolet Rays

Substances

  • Antimicrobial Cationic Peptides
  • Collagen Type I
  • CopA3 peptide, Copris tripartitus
  • Insect Proteins
  • Matrix Metalloproteinase 1