Rohit, AC and Sathisha, K and Aparna, HS (2012) A variant peptide of buffalo colostrum beta-lactoglobulin inhibits angiotensin I-converting enzyme activity. In: EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY, 53 . pp. 211-219.
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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.
|Item Type:||Journal Article|
|Additional Information:||Copy right for this article belongs to Elsevier Masson SAS|
|Keywords:||Bubalus bubalis;Colostrum;beta-Lactoglobulin;De nova sequencing;Angiotensin I-converting enzyme|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||03 Aug 2012 05:12|
|Last Modified:||03 Aug 2012 05:13|
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