Arpitha, A. and Brijesha, N. and Aparna, H. S. (2019) Discovery, synthesis, and <i>in vitro</i> evaluation of a novel bioactive peptide for ACE and DPP-IV inhibitory activity. European Journal of Medicinal Chemistry, 180. pp. 99-110. ISSN 1768-3254
Full text not available from this repository. (Request a copy)Abstract
Biologically active or bioactive peptides are unique amino acid sequences found encrypted in food proteins. These peptides, upon hydrolysis, can exert positive physiological effects on human health, different from that of their native protein. These effects are brought about by their interaction with specific targets in the body, thereby, mimicking physiologically relevant peptides. Peptides are derived from food proteins, they are popular natural alternatives for the management of common metabolic disorders. In the present study, we aimed to identify bioactive peptide sequences (less than 3 kDa) from fat globule membrane protein (FGMP) hydrolysates of buffalo colostrum using a combination of empirical, computational and in vitro methods. The empirical approach aided in the identification of 89 FGMP peptides (m/z-415 to 2939) which were annotated and profiled for bioactivity. Few lead peptides were analyzed by molecular docking for the inhibitory potential of Angiotensin Converting Enzyme (ACE) and Dipeptidyl Peptidase-IV (DPP-IV). A heptapeptide (m/z-723.3) synthesized was found to inhibit ACE (IC50: 74.27 mu M) and DPP-IV (IC50: 3.83 mM). (C) 2019 Elsevier Masson SAS. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | Buffalo colostrum; FGMP; Bioactive peptide; ACE; DPP-IV |
| Subjects: | B Life Science > Biotechnology |
| Divisions: | Department of > Biotechnology |
| Depositing User: | C Swapna Library Assistant |
| Date Deposited: | 13 Dec 2023 05:25 |
| Last Modified: | 13 Dec 2023 05:25 |
| URI: | http://eprints.uni-mysore.ac.in/id/eprint/17779 |
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