Multifunctional Properties of BMAP-18 and Its Aliphatic Analog against Drug-Resistant Bacteria

BMAP-18, derived from the N-terminal region of bovine myeloid antimicrobial peptide BMAP-27, demonstrates potent activity without cytotoxicity. This study aimed to compare antibacterial, antibiofilm, and anti-inflammatory properties rich in aromatic phenylalanine residues, with its aliphatic analog, BMAP-18-FL. Both BMAP-18 BMAP-18-FL exhibited equally activities against Gram-positive Gram-negative bacteria, particularly methicillin-resistant Staphylococcus aureus (MRSA) multidrug-resistant Pseudomonas aeruginosa (MDRPA). Mechanistic investigations employing SYTOX green uptake, DNA binding, FACScan analysis revealed that both peptides acted by inducing membrane permeabilization subsequent intracellular targeting. Moreover, effectively prevented biofilm formation eradicated existing biofilms MRSA MDRPA. Notably, displayed a superior compared significantly reducing expression levels pro-inflammatory cytokines lipopolysaccharide-stimulated macrophages. emphasizes similarities differences antimicrobial, between BMAP-18-FL, providing valuable insights for development multifunctional drug-resistant bacteria.