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.

• Periodical: Materials Science Forum (Volume 1077)
• Pages: 131-143
• DOI: https://doi.org/10.4028/p-h6246e
• Online since: December 2022
• Authors: Nur Suraya Abd Wahab, Emmy Liza Anak Yaji, Norfahana Abd Talib, Mohamad Zulkeflee Sabri, Kelly Tau Len Yong, Nadia Razali, Khairul Faizal Pa'ee*
• Keywords: Angiotensin-I Converting Enzyme (ACE), Autodoc Vina, Bioactive Peptides, Bioinformatics, BIOPEP, Molecular Docking

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