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Xiaochang WANG


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Journal of Zhejiang University SCIENCE B 2021 Vol.22 No.7 P.575-589


Inhibitory mechanism of angiotensin-converting enzyme inhibitory peptides from black tea

Author(s):  Yating LU, Yu WANG, Danyi HUANG, Zhuang BIAN, Peng LU, Dongmei FAN, Xiaochang WANG

Affiliation(s):  Tea Research Institute, College of Agriculture and Biotechnology, Zhejiang University, Hangzhou 310058, China; more

Corresponding email(s):   xcwang@zju.edu.cn

Key Words:  Black tea, Angiotensin-1-converting enzyme (ACE) inhibitory peptide, Kinetic study, Molecular docking, Molecular dynamic (MD) simulation

Yating LU, Yu WANG, Danyi HUANG, Zhuang BIAN, Peng LU, Dongmei FAN, Xiaochang WANG. Inhibitory mechanism of angiotensin-converting enzyme inhibitory peptides from black tea[J]. Journal of Zhejiang University Science B, 2021, 22(7): 575-589.

@article{title="Inhibitory mechanism of angiotensin-converting enzyme inhibitory peptides from black tea",
author="Yating LU, Yu WANG, Danyi HUANG, Zhuang BIAN, Peng LU, Dongmei FAN, Xiaochang WANG",
journal="Journal of Zhejiang University Science B",
publisher="Zhejiang University Press & Springer",

%0 Journal Article
%T Inhibitory mechanism of angiotensin-converting enzyme inhibitory peptides from black tea
%A Yating LU
%A Danyi HUANG
%A Zhuang BIAN
%A Peng LU
%A Dongmei FAN
%A Xiaochang WANG
%J Journal of Zhejiang University SCIENCE B
%V 22
%N 7
%P 575-589
%@ 1673-1581
%D 2021
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B2000520

T1 - Inhibitory mechanism of angiotensin-converting enzyme inhibitory peptides from black tea
A1 - Yating LU
A1 - Yu WANG
A1 - Danyi HUANG
A1 - Zhuang BIAN
A1 - Peng LU
A1 - Dongmei FAN
A1 - Xiaochang WANG
J0 - Journal of Zhejiang University Science B
VL - 22
IS - 7
SP - 575
EP - 589
%@ 1673-1581
Y1 - 2021
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B2000520

The aim of this work is to discover the inhibitory mechanism of tea peptides and to analyse the affinities between the peptides and the angiotensin-converting enzyme (ACE) as well as the stability of the complexes using in vitro and in silico methods. Four peptide sequences identified from tea, namely peptides I, II, III, and IV, were used to examine ACE inhibition and kinetics. The half maximal inhibitory concentration (IC50) values of the four peptides were (210.03±18.29), (178.91±5.18), (196.31±2.87), and (121.11±3.38) μmol/L, respectively. The results of Lineweaver-Burk plots showed that peptides I, II, and IV inhibited ACE activity in an uncompetitive manner, which requires the presence of substrate. Peptide III inhibited ACE in a non-competitive manner, for which the presence of substrate is not necessary. The docking simulations showed that the four peptides did not bind to the active sites of ACE, indicating that the four peptides are allosteric inhibitors. The binding free energies calculated from molecular dynamic (MD) simulation were -72.47, -42.20, -52.10, and -67.14 kcal/mol (1 kcal=4.186 kJ), respectively. The lower IC50 value of peptide IV may be attributed to its stability when docking with ACE and changes in the flexibility and unfolding of ACE. These four bioactive peptides with ACE inhibitory ability can be incorporated into novel functional ingredients of black tea.


方法:用体外酶抑制实验获取茶叶多肽(红茶中分离)对ACE的半抑制浓度(IC50);用酶动力学实验探究红茶多肽对ACE的抑制类型;通过分子对接技术预测茶叶多肽在ACE蛋白中的结合位置;通过100 ns的分子动力学模拟实验评价各多肽对ACE蛋白自由度和展开度的影响以及多肽-蛋白结合物的稳定性。


Darkslateblue:Affiliate; Royal Blue:Author; Turquoise:Article


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