期刊
JOURNAL OF CEREAL SCIENCE
卷 60, 期 1, 页码 92-98出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jcs.2014.01.019
关键词
Gluten; ACE-inhibitory peptide; Docking simulation
资金
- Research Council of Ferdowsi University of Mashhad
- Research Council of Mashhad Branch, Islamic Azad University
The present study was carried out to characterize ACE inhibitory peptides which are released from the trypsin hydrolysate of wheat gluten protein. In silico proteolitic digestion of a high molecular weight glutenin subunit was performed. Among the resultant fragments, four peptides were selected for chemical synthesis based on the chemoinformatics studies and docking properties. The ACE inhibitory activity and kinetic parameters of the most important peptides were determined. Molecular docking simulation was also performed to predict the sites on ACE in which these peptides bind and displayed inhibition mechanisms. Two peptide sequences of IPALLKR (P4) and AQQLAAQLPAMCR (P6) showed higher ACE inhibitory activity among peptide collection. The IC50 values of P6 and P4 were 43 +/- 1.3 mu M and 68 +/- 2.8 mu M, respectively. P6 peptide was proved to be a more potent ACE inhibitor than P4 peptide. Lineweaver-Burk plots revealed that P6 and P4 behaved as non-competitive and competitive ACE inhibitors, respectively. The simulations showed that P4 bound to the active site region. Conversely, P6 bound to the N-terminus entrance of substrate tunnel and obstructed the substrate access into the catalytic site. Overall, the results showed that these peptides would be considered as a model for discovering new bio-compatible ACE inhibitors. (C) 2014 Elsevier Ltd. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据