Hypotensive effect of potent angiotensin-I-converting enzyme inhibitory peptides from corn gluten meal hydrolysate: Gastrointestinal digestion and transepithelial transportation modifications

被引：0

作者：

Chanajon, Phiromya ^{[1
]}

Hamzeh, Ali ^{[1
]}

Tian, Fu ^{[2
]}

Roytrakul, Sittiruk ^{[3
]}

Oluwagunwa, Olayinka A. ^{[4
]}

Kadam, Deepak ^{[4
]}

Aluko, Rotimi E. ^{[4
]}

Aueviriyavit, Sasitorn ^{[5
]}

Wongwanakul, Ratjika ^{[5
]}

Yongsawatdigul, Jirawat ^{[1
]}

机构：

[1] School of Food Technology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima,30000, Thailand

[2] College of Food and Pharmaceutical Engineering, Guizhou Institute of Technology, Guiyang,550000, China

[3] National Center for Genetic Engineering and biotechnology, Pathumthani, 12120, Thailand

[4] Department of Food and Human Nutritional Sciences, University of Manitoba, Winnipeg,MB,R3T 2N2, Canada

[5] National Nanotechnology Center, National Science and Technology Development Agency, 111 Thailand Science Park, Pathum Thani,12120, Thailand

来源：

Food Chemistry | 2025年 / 462卷

关键词：

Blood pressure - Molecular dynamics - Peptides;

D O I：

10.1016/j.foodchem.2024.140953

中图分类号：

学科分类号：

摘要：

The study examined the antihypertensive effect of peptides derived from pepsin-hydrolyzed corn gluten meal, namely KQLLGY and PPYPW, and their in silico gastrointestinal tract digested fragments, KQL and PPY, respectively. KQLLGY and PPYPW showed higher angiotensin I-converting enzyme (ACE)-inhibitory activity and lower ACE inhibition constant (Ki) values when compared to KQL and PPY. Only KQL showed a mild antihypertensive effect in spontaneously hypertensive rats with −7.83 and − 5.71 mmHg systolic and diastolic blood pressure values, respectively, after 8 h oral administration. During passage through Caco-2 cells, KQL was further degraded to QL, which had reduced ACE inhibitory activity. In addition, molecular dynamics revealed that the QL-ACE complex was less stable compared to the KQL-ACE. This study reveals that structural transformation during peptide permeation plays a vital role in attenuating antihypertensive effect of the ACE inhibitor peptide. © 2024

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