The
antimicrobial activity of bovine bactericidal / permeability-increasing
protein (bBPI)-derived synthetic peptides against
mastitis-causing
Gram-negative
bacteria was evaluated. Three peptides were synthesized with sequences corresponding to amino acids 65-99 (bBPI65-99), 142-169 (bBPI142-169), or the combination of amino acids 90-99 and 148-161 (bBPI90-99,148-161) of bBPI. The bBPI90-99,148-161
peptide demonstrated the widest spectrum of
antimicrobial activity, with minimum inhibitory (MIC) and bactericidal (MBC) concentration values
ranging from 16-64 μg / ml against
Escherichia coli,
Klebsiella pneumoniae, and
Enterobacter spp, and 64-128 μg / ml against
Pseudomonas aeruginosa. None of the peptides exhibited any
growth inhibitory effect on
Serratia marcescens. The
antimicrobial activity of bBPI90-99,148-161 was inhibited in milk, but preserved in serum. Finally, both bBPI142-169 and bBPI90-99,148-161 were demonstrated to completely neutralize LPS. The
peptide bBPI90-99,148-161 is a potent neutralizer of the highly pro-inflammatory molecule bacterial LPS and has antimicrobial activity against a variety of
Gram-negative
bacteria.