Structure-Activity Relationship of Synthetic Variants of the Milk-Derived Antimicrobial Peptide αs2-Casein f(183–207)

摘要: Template-based studies on antimicrobial peptide (AMP) derivatives obtained through manipulation of the amino acid sequence are helpful to identify properties or residues that important for biological activity. The present study sheds light importance specific acids milk-derived αs2-casein f(183–207) its antibacterial activity against food-borne pathogens Listeria monocytogenes and Cronobacter sakazakii. Trimming revealed at C-terminal end Removal last 5 replacement Arg position 23 by an Ala residue significantly decreased These findings suggest Arg23 is very optimal peptide. Substitution also positively charged Lys positions 15 17 caused a significant reduction effectiveness C. sakazakii, which points toward positive charge Indeed, simultaneous various was linked loss bactericidal On other hand, Pro 14 20 resulted in increased potency, hydrophobic tagging f(193–203) f(197–207) peptides with multiple Trp Phe their potency L. monocytogenes. Finally, effect pH (4.5 7.4), temperature (4°C 37°C), addition sodium calcium salts (1% 3%) 15-amino-acid f(193–207) determined, shown be completely abolished high-saline environments.