Activity Prediction and Molecular Mechanism of Bovine Blood Derived Angiotensin I-Converting Enzyme Inhibitory Peptides

被引：15
|
作者：
Zhang, Ting [1 ]
Nie, Shaoping [2 ]
Liu, Boqun [1 ]
Yu, Yiding [1 ]
Zhang, Yan [1 ]
Liu, Jingbo [1 ]
机构：
[1] Jilin Univ, Lab Nutr & Funct Food, Changchun 130023, Jilin, Peoples R China
[2] Nanchang Univ, State Key Lab Food Sci & Technol, Nanchang, Jiangxi, Peoples R China
来源：
PLOS ONE | 2015年 / 10卷 / 03期
基金：
中国国家自然科学基金;
关键词：
BIOACTIVE PEPTIDES; IDENTIFICATION; PROTEIN; QSAR; DIGESTION; PURIFICATION; HEMOGLOBIN; MODEL; MILK; MEAT;
D O I：
10.1371/journal.pone.0119598
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Development of angiotensin I-converting enzyme (ACE, EC 3.4.15.1) inhibitory peptides from food protein is under extensive research as alternative for the prevention of hypertension. However, it is difficult to identify peptides released from food sources. To accelerate the progress of peptide identification, a three layer back propagation neural network model was established to predict the ACE-inhibitory activity of pentapeptides derived from bovine hemoglobin by simulated enzyme digestion. The pentapeptide WTQRF has the best predicted value with experimental IC50 23.93 mu M. The potential molecular mechanism of the WTQRF / ACE interaction was investigated by flexible docking.
引用
收藏
页数：13
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