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Research Article | Open Access

Novel ACE-inhibiting peptides from soybean protein hydrolysates by peptidomics combined with in silico analysis and their inhibitory effects on proliferation and migration of Ang II-induced VSMCs

Tian-Tian Zhang1, Qiao-Lin Cai1, Zhen-Yu Gu1,2, Tian-Yuan Song1,2( )
School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, China
Key Laboratory for Food Microbial Technology of Zhejiang Province, College of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, China
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Highlights

(1) Sixty-eight target peptides were identified by peptidomics and assessed potential properties.

(2) The WGPRL, a non-competitive inhibitor to ACE, was assessed ADMET characteristics.

(3) The WGPRL attenuated the Ang II-induced over-proliferation and migration of VSMCs.

Graphical Abstract

Peptide sequences from soybean protease hydrolysates were identified by high-throughput peptidomics technology. Combined with ACE inhibition activity and structure-activity relationship (SAR) -based computer simulation system, potential active peptides in the enzymatic hydrolysates were rapidly screened. A novel soybean antihypertensive peptide WGPRL with high ACE inhibitory activity and inhibitory effect on Ang II-induced VSMC proliferation and migration was identified by peptidomics.

Abstract

Soybean protease hydrolysate (SPH) contains abundant antihypertensive peptides, yet the sequence defining vital antihypertensive peptides is unclear. Peptiomics sequencing analyzed peptides in enzymatic products from soybean protein alkaline and flavor proteases. Database queries and simulations screened key peptide monomers, assessing angiotensin-converting enzyme (ACE) inhibitory activities in vitro. Peptidomics identified 6,980 short peptides in SPH, predominantly hydrophobic at the N-terminal. Sixty-eight were target peptides, assessed for allergenicity, toxicity, and physicochemical properties. Pentapeptide WGPRL and tetrapeptide WLRL exhibited optimal ACE inhibition, deemed non-competitive. ADMET characteristics indicated good water solubility and human intestinal absorption, suggesting potential as peptide drugs or functional food ingredients. The impact of a novel antihypertensive peptide on Ang II-induced vascular smooth muscle cell dysfunction was explored. WGPRL and WLRL significantly inhibited Ang II-induced vascular smooth muscle cell over-proliferation and migration. These findings indicated that the potent antihypertensive SPH was enriched with a novel pentapeptide WGPRL and has potential as effective components of antihypertensive peptides functional food.

Keywords

antihypertensive peptidessoybean proteinpeptidomicsADMET characteristicsvascular smooth muscle cells

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Food & Medicine Homology
Volume 1 Issue 2,
December 2024
Article number: 9420023
DOI: 10.26599/FMH.2024.9420023

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Cite this article:
Zhang T-T, Cai Q-L, Gu Z-Y, et al. Novel ACE-inhibiting peptides from soybean protein hydrolysates by peptidomics combined with in silico analysis and their inhibitory effects on proliferation and migration of Ang II-induced VSMCs. Food & Medicine Homology, 2024, 1(2): 9420023. https://doi.org/10.26599/FMH.2024.9420023

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Received: 17 June 2024
Revised: 11 July 2024
Accepted: 11 July 2024
Published: 15 August 2024
© National R & D Center for Edible Fungus Processing Technology 2024. Published by Tsinghua University Press.

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).