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

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.