A variant peptide of buffalo colostrum β-lactoglobulin inhibits angiotensin I-converting enzyme activity

被引：69

作者：

Rohit, A. C. ^{[1
]}

Sathisha, K. ^{[2
]}

Aparna, H. S. ^{[1
]}

机构：

[1] Univ Mysore, Dept Studies Biotechnol, Mysore 570006, Karnataka, India

[2] Indian Inst Sci, Mol Biophys Unit, Bangalore 560012, Karnataka, India

来源：

EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY | 2012年 / 53卷

关键词：

Bubalus bubalis; Colostrum; beta-Lactoglobulin; De nova sequencing; Angiotensin I-converting enzyme; DISSOCIATION MASS-SPECTROMETRY; BIOACTIVE PEPTIDES; SEQUENCE-ANALYSIS; BUBALUS-BUBALIS; MILK; BINDING; IDENTIFICATION; PROTEINS; GROWTH; CDNA;

D O I：

10.1016/j.ejmech.2012.03.057

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

beta-lactoglobulin is a rich source of bioactive peptides. The LC-MS separated tryptic peptides of buffalo colostrum beta-lactoglobulin (BLG-col) were computed based on MS-MS fragmentation for de novo sequencing. Among the selected peptides (P1-P8), a variant was detected with methionine at position 74 instead of glutamate. The sequences of two peptides were identical to hypocholesterolemic peptides whereas the remaining peptides were in accordance with buffalo milk beta-lactoglobulin. Comparative sequence analysis of BLG-col to milk beta-lactoglobulin was carried out using CLUSTALW2 and a molecular model for BLG-col was constructed (PMDB ID-PM0076812). The synthesized variant pentapeptide (IIAMK, m/z-576 Da) was found to inhibit angiotensin I-converting enzyme (ACE) with an IC50 of 498 +/- 2 mu M, which was rationalized through docking simulations using Molgrow virtual docker. (C) 2012 Elsevier Masson SAS. All rights reserved.

引用

页码：211 / 219

页数：9

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