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Generation, characterization and molecular binding mechanism of novel dipeptidyl peptidase-4 inhibitory peptides from sorghum bicolor seed protein.

Abdul, Majid and Lakshmikanth, M. and Lokanath, N.K. and Poornima Priyadarshini, C. G. (2022) Generation, characterization and molecular binding mechanism of novel dipeptidyl peptidase-4 inhibitory peptides from sorghum bicolor seed protein. Food Chemistry, 369. p. 130888. ISSN 0308-8146

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Abstract

Food proteins and their constituent peptides impart huge health benefits besides their nutritional attributes. Sorghum bicolor protein hydrolysates (SPH) and derived bioactive peptides generated by simulated gastrointestinal digestion were studied for DPP-4 inhibitory properties using in vitro and in situ assays. Identified peptides, LSICGEESFGTGSDHIR (PEP1), SLGESLLQEDVEAHK (PEP2) and QLRDIVDK (PEP4) displayed potent DPP-4 inhibition with IC50 values of 73.5, 82.5 and 8.55 μM respectively. DPP-4 inhibition mechanism by the peptides was investigated by DPP4-peptide inhibition kinetics, molecular docking and microscale thermophoresis binding studies. The peptides bound to DPP-4 with micromolar affinities and PEP4 showed significantly increased affinity. The mixed type enzyme inhibition by peptides suggested that the peptides either block the active site of DPP-4 or changes the enzyme conformation via a secondary binding site. Overall, the results demonstrate that sorghum seeds are an adequate source of peptides with DPP-4 inhibitory properties that could be used in functional food formulations.

Item Type: Article
Uncontrolled Keywords: Sorghum bicolor DPP-4 Bioactive peptides Gastrointestinal simulation Molecular docking Microscale thermophoresis Mixed type enzyme kinetics Diabetes
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 25 Peptide Chemistry
600 Technology > 08 Food technology > 21 Cereals > 06 Sorghum
Divisions: Molecular Nutrition
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 23 Nov 2021 10:40
Last Modified: 23 Nov 2021 10:40
URI: http://ir.cftri.res.in/id/eprint/15073

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