Structure-activity Relationships of αs-casein Peptides with Multifunctional Biological Activities

Overview

Journal Mol Cell Biochem

Publisher Springer

Specialty Biochemistry

Date 2013 Aug 22

PMID 23963991

Citations 5

Authors

Srinivas Sistla

Affiliations

Soon will be listed here.

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 α-S2 casein f (79-88) and α-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.

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