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

Rohit, A. C. and Sathisha, K. and Aparna, H. S. (2012) A variant peptide of buffalo colostrum β-lactoglobulin inhibits angiotensin I-converting enzyme activity. European Journal of Medicinal Chemistry, 53. 211 - 219. ISSN 1768-3254

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Official URL: https://doi.org/10.1016/j.ejmech.2012.03.057

Abstract

β-lactoglobulin is a rich source of bioactive peptides. The LC-MS separated tryptic peptides of buffalo colostrum β-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 β-lactoglobulin. Comparative sequence analysis of BLG-col to milk β-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 μM, which was rationalized through docking simulations using Molgrow virtual docker.

Item Type: Article
Uncontrolled Keywords: Colostrum, β-Lactoglobulin, Sequencing, Angiotensin I-converting enzyme
Subjects: B Life Science > Biotechnology
Divisions: Department of > Biotechnology
Depositing User: MUL SWAPNA user
Date Deposited: 19 Jul 2019 05:07
Last Modified: 19 Jul 2019 05:07
URI: http://eprints.uni-mysore.ac.in/id/eprint/5355

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