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Updated: May 8, 2026

Sigma's Non-specific Protease Activity Assay - Casein as a Substrate
Published on: September 17, 2008
Structure-activity relationships of αs-casein peptides with multifunctional biological activities
1Department of Protein Chemistry and Technology, Central Food Technological Research Institute (CSIR), Mysore, 570020, Karnataka, India, sistlasrinivas@gmail.com.
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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