Molecular docking and pharmacokinetics properties of active peptide derived from fish collagen as Matrix metalloproteinase-9 (MMP-9) inhibitor for wound healing application
Heli Siti Halimatul Munawaroh, Gun Gun Gumilar, Faradhina Salfa Nindya, Selmi Fiqhi Khoiriah

Program Studi Kimia, Universitas Pendidikan Indonesia

Abstract

Matrix metalloproteinase-9 (MMP-9) is one of the members of zinc-dependent endopeptidase that is responsible for extracellular matrix (ECM) remodelling during skin wound repair. Inhibiting the MMP-9 activities can promote the wound repair process and prevent chronic wounds. The in silico approach provides high throughput screening of promising potential inhibitors for MMP-9. The natural inhibitors were derived from in silico hydrolysis of Salmo salar fish collagen. The toxicity and allergenicity tests were evaluated to select active peptides that are nontoxic and nonallergenic. It was found several active peptides, such as WF (Trp-Phe), YW (Tyr-Trp), SWY (Ser-Trp-Tyr), PM (Pro-Met), GGG (Gly-Gly-Gly), VW (Val-Trp), FQ (Phe-Gln), FT (Phe-Thr), HF (His-Phe), FR (Phe-Arg), HFR (His-Phe-Arg), CF (Cys-Phe), have good binding interactions with MMP-9. All of the peptides may be considered as MMP-9 inhibitors. For assessing the effect of these peptides, the pharmacokinetics analysis was carried out using SWISSADME in order to design novel bioactive candidates of MMP-9. The results show the in silico drug design approach has notorious peptides that have high binding affinities and exhibit favorable pharmacokinetics profiles. In vitro and in vivo clinical trials should be conducted to support the in silico findings.

Keywords: MMP-9, inhibitor, matrix metaloproteinase, peptida aktif

Topic: Chemistry