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

• Published in: Molecules (Basel, Switzerland) Vol. 19; no. 5; pp. 6407 - 6414
• Main Authors: Kim, Dong-Hee, Kim, Han-Hyuk, Kim, Hyeon-Jeong, Jung, Hyun-Gug, Yu, Jae-Myo, Lee, Eun-Su, Cho, Yong-Hun, Kim, Dong-In, An, Bong-Jeun
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI 20.05.2014; MDPI AG
• Subjects: Antimicrobial Cationic Peptides - pharmacology; CCD-986sk cells; Cells, Cultured; Collagen Type I - antagonists & inhibitors; Collagen Type I - radiation effects; CopA3; Copris tripartitus; Dose-Response Relationship, Drug; Fibroblasts - drug effects; Fibroblasts - metabolism; Fibroblasts - radiation effects; Insect Proteins - pharmacology; Matrix Metalloproteinase 1 - genetics; Matrix Metalloproteinase 1 - metabolism; matrix metalloproteinase-1; Skin - cytology; Skin - metabolism; Skin - radiation effects; Skin Aging - drug effects; ultraviolet; Ultraviolet Rays
• ISSN: 1420-3049; 1420-3049
• DOI: 10.3390/molecules19056407

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.