Molecular Interaction of Angiotensin-I Converting Enzyme (ACE) with Peptides Derived from Collagen Type i as Analogue for Tilapia By-Product Protein Precursor

Abstract

The study aimed to investigate the molecular interaction of ACE-inhibitory peptides derived from collagen type I. Collagen type I alpha 1 and alpha 2 were used in this work was to analogue the tilapia by-product protein precursor for ACE-inhibitory peptides production. In silico production of ACE-inhibitory peptides derived collagen type I from BIOPEP was used to simulate peptide-ACE interaction using Autodock Vina. Most potent ACE-inhibitory tri-and di-peptides, Gly-Leu-Pro (GLP IC50 1.62 μM) and Cys-Phe (CF IC50 1.96 μM) derived alpha 1 and Leu-Gly-Pro (LGP IC50 0.72 μM), and Glu-Tyr (EY IC50 2.68 μM) derived alpha 2 were chosen from BIOPEP database. The hydrophobicity of the amino acids is suggested to contribute to bioactivity. These peptides inhibited the active sites of ACE at the C terminal residue. The zinc (II) interacted with all four peptides directly and indirectly. GLP and CY of alpha 1 could share a bond with His 383, His 387, and Glu 411 instead of directly binding to the zinc (II) atom. ACE has a zinc ion in its coordinates with His 383, His 387, and Glu 411. Alpha 2's LGP and EY were directly bound to Zinc (ii) atoms.