Enzyme inhibition kinetics and molecular interactions of patatin peptides with angiotensin I-converting enzyme and renin

被引:75
|
作者
Fu, Yu [1 ]
Alashi, Adeola M. [2 ]
Young, Jette F. [1 ]
Therkildsen, Margrethe [1 ]
Aluko, Rotimi E. [2 ]
机构
[1] Aarhus Univ, Dept Food Sci, Blichers Allee 20, DK-8830 Tjele, Denmark
[2] Univ Manitoba, Dept Human Nutr Sci, Winnipeg, MB R3T 2N2, Canada
关键词
ACE; Renin; Patatin peptides; Kinetics; Molecular docking; ANTIHYPERTENSIVE PEPTIDES; MECHANISM; VITRO; IDENTIFICATION; PURIFICATION; TRIPEPTIDES; DOCKING; SYSTEM; DRUGS;
D O I
10.1016/j.ijbiomac.2017.03.054
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In this work, the inhibitory effects of potato patatin-derived peptides Trp-Gly (WG) and Pro-Arg-Tyr (PRY) on angiotensin I-converting enzyme (ACE) and renin activities were investigated using kinetics, intrinsic fluorescence and molecular docking. The results indicated that PRY was a more potent ACE- and renin-inhibitory peptide than WG. Enzyme inhibition kinetics showed that WG and PRY inhibited ACE activity through mixed-type and competitive modes, respectively. The inhibitory mechanism of WG and PRY towards renin was determined to be mixed-type. PRY exhibited stronger affinity towards ACE and renin molecules, when compared to WG as determined by intrinsic fluorescence intensity. Molecular docking data confirmed that the higher inhibitory potency of PRY might be attributed to formation of more hydrogen bonds with the enzyme's active site or non-active sites that distorted the configuration necessary for catalysis. (C) 2017 Elsevier B.V. All rights reserved.
引用
收藏
页码:207 / 213
页数:7
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