Novel Angiotensin-Converting Enzyme-Inhibitory Peptides Obtained from : Preparation, Identification and Potential Antihypertensive Mechanism

Overview

Journal Biomolecules

Publisher MDPI

Specialties Biochemistry
Molecular Biology

Date 2024 May 24

PMID 38785988

Authors

Jiaming Cao

Boyuan Xiang

Baojie Dou

Jingfei Hu

Lei Zhang

Xinxin Kang

Mingsheng Lyu

Shujun Wang

Affiliations

Soon will be listed here.

Abstract

Peptides possessing antihypertensive attributes via inhibiting the angiotensin-converting enzyme (ACE) were derived through the enzymatic degradation of (ribbonfish) using alkaline protease. The resulting mixture underwent filtration using centrifugation, ultrafiltration tubes, and Sephadex G-25 gels. Peptides exhibiting ACE-inhibitory properties and DPPH free-radical-scavenging abilities were isolated and subsequently purified via LC/MS-MS, leading to the identification of over 100 peptide components. In silico screening yielded five ACE inhibitory peptides: FAGDDAPR, QGPIGPR, IFPRNPP, AGFAGDDAPR, and GPTGPAGPR. Among these, IFPRNPP and AGFAGDDAPR were found to be allergenic, while FAGDDAPRR, QGPIGPR, and GPTGPAGP showed good ACE-inhibitory effects. IC values for the latter peptides were obtained from HUVEC cells: FAGDDAPRR (IC = 262.98 μM), QGPIGPR (IC = 81.09 μM), and GPTGPAGP (IC = 168.11 μM). Peptide constituents derived from ribbonfish proteins effectively modulated ACE activity, thus underscoring their therapeutic potential. Molecular docking and modeling corroborated these findings, emphasizing the utility of functional foods as a promising avenue for the treatment and prevention of hypertension, with potential ancillary health benefits and applications as substitutes for synthetic drugs.

Citing Articles

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