Quantitative Structure Activity Relationship of Angiotensin Ⅰ-Converting Enzyme Inhibitory Tripeptides Derived from Food Proteins

doi:10.7506/spkx1002-6630-201309005

Abstract

Abstract:

Based on published IC50 values, a quantitative structure activity relationship (QSAR) model indicating
the relationship between amino acid sequences and inhibitory activity was developed for angiotensin Ⅰ-converting
enzyme (ACE) inhibitory tripeptides derived from food proteins. The following QSAR model for IC50 versus
hydrophilicity and steric and electronic properties (X3) of amino acid side chains was developed: Y = 1.952 +
0.1229X2 + 0.0924X3 + 0.0425X5 + 0.1777X7 + 0.136X8－0.0809X9－0.1763X10. According to this model, amino
acids with low hydrophilicity and low steric parameters such as Val, Leu and Ile preferably existed at the first site
near the N terminus, those with low hydrophilicity and low charge parameters such as Lys and Arg at the second
site, and those with low hydrophilicity and high steric parameters such as Pro and Phe at the third site. In the
prediction of the tripeptides VNP, VWP and VAP for IC50, an error varying from 0.06 to 0.23 was obtained between
the experimental and predicted values, which was within the range of model samples. Thus, the described mode has
good prediction capability.

Key words: angiotensin Ⅰ-converting enzyme (ACE), tripeptide, quantitative structure activity relationship (QSAR)

CLC Number:

R933.7

CHEN Ji-wang1，LIU Shan-shan1，CAI Guang-xia1，WU Yong-ning1,2. Quantitative Structure Activity Relationship of Angiotensin Ⅰ-Converting Enzyme Inhibitory Tripeptides Derived from Food Proteins[J]. FOOD SCIENCE, 2013, 34(9): 19-23.

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