Jahan, I.; Kumar, S.D.; Shin, S.Y.; Lee, C.W.; Shin, S.-H.; Yang, S. Multifunctional Properties of BMAP-18 and Its Aliphatic Analog against Drug-Resistant Bacteria. Pharmaceuticals2023, 16, 1356.
Jahan, I.; Kumar, S.D.; Shin, S.Y.; Lee, C.W.; Shin, S.-H.; Yang, S. Multifunctional Properties of BMAP-18 and Its Aliphatic Analog against Drug-Resistant Bacteria. Pharmaceuticals 2023, 16, 1356.
Jahan, I.; Kumar, S.D.; Shin, S.Y.; Lee, C.W.; Shin, S.-H.; Yang, S. Multifunctional Properties of BMAP-18 and Its Aliphatic Analog against Drug-Resistant Bacteria. Pharmaceuticals2023, 16, 1356.
Jahan, I.; Kumar, S.D.; Shin, S.Y.; Lee, C.W.; Shin, S.-H.; Yang, S. Multifunctional Properties of BMAP-18 and Its Aliphatic Analog against Drug-Resistant Bacteria. Pharmaceuticals 2023, 16, 1356.
Abstract
BMAP-18, derived from the N-terminal region of bovine myeloid antimicrobial peptide BMAP-27, demonstrated potent antimicrobial activity without cytotoxicity. This study aimed to compare the antibacterial, antibiofilm, and anti-inflammatory properties of BMAP-18, rich in aromatic phenylalanine residues, with its aliphatic analogue, BMAP-18-FL. Both aromatic BMAP-18 and aliphatic BMAP-18-FL exhibited equally potent antimicrobial activities against Gram-positive and Gram-negative bacteria, particularly methicillin-resistant Staphylococcus aureus (MRSA) and multidrug-resistant Pseudomonas aeruginosa (MDRPA). Mechanistic investigations employing SYTOX green uptake, DNA binding, and FACScan analysis revealed that both peptides acted by inducing membrane permeabilization and subsequent intracellular targeting. Moreover, both BMAP-18 and BMAP-18-FL effectively prevented biofilm formation and eradicated existing biofilms of MRSA and MDRPA. Notably, BMAP-18-FL displayed superior anti-inflammatory activity compared to BMAP-18, significantly reducing the expression levels of pro-inflammatory cytokines in lipopolysaccharide-stimulated macrophages. This study emphasizes the similarities and differences in the antimicrobial, antibiofilm, and anti-inflammatory properties between aromatic BMAP-18 and aliphatic BMAP-18-FL, providing valuable insights for the development of multifunctional antimicrobial peptides against drug-resistant bacteria.
Keywords
antimicrobial peptide; drug-resistant bacteria; cathelicidin; multifunction; aromatic and aliphatic residue
Subject
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
