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Structure–activity relationships of as-casein peptides with multifunctional biological activities

Srinivas, S. (2013) Structure–activity relationships of as-casein peptides with multifunctional biological activities. Molecular and Cellular Biochemistry, 384. pp. 29-38.

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Abstract

Multifunctional bioactive peptides have a wider role in modulating physiological functions and possess multiple biological activities. Peptides from bovine milk with sequences QKALNEINQF [p10] and TKKTKLTEEEKNRL [p14] from a-S2 casein f (79–88) and a-S2 casein f (148–161) were identified to be having multifunctional biological activities and were synthesized. These synthesized peptides show various biological activities like angiotensin-converting enzyme inhibition, prolyl endopeptidase inhibition, antioxidant, and antimicrobial activities. The mode of antimicrobial mechanism was studied and p10 shows depolarization of cell membrane, whereas p14 was found to display DNA-binding activity. Structural studies envisaged backbone flexibility, for differences in their mode of action. Peptide structure function studies were correlated to understand their multifunctional biological activity.

Item Type: Article
Uncontrolled Keywords: Peptides � Casein � Multifunctional � Circular dichroism � DNA binding � Antiulcer � Antihypertensive � Antimicrobial
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 25 Peptide Chemistry
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 08 Dec 2016 06:10
Last Modified: 08 Dec 2016 06:10
URI: http://ir.cftri.com/id/eprint/12577

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