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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 antimicrobial activity without cytotoxicity. This study aimed to compare the antibacterial, antibiofilm, and anti-inflammatory properties of BMAP-18, rich in aromatic phenylalanine residu...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10609797/ https://www.ncbi.nlm.nih.gov/pubmed/37895827 http://dx.doi.org/10.3390/ph16101356 |
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author | Jahan, Ishrat Kumar, Sukumar Dinesh Shin, Song Yub Lee, Chul Won Shin, Sung-Heui Yang, Sungtae |
author_facet | Jahan, Ishrat Kumar, Sukumar Dinesh Shin, Song Yub Lee, Chul Won Shin, Sung-Heui Yang, Sungtae |
author_sort | Jahan, Ishrat |
collection | PubMed |
description | BMAP-18, derived from the N-terminal region of bovine myeloid antimicrobial peptide BMAP-27, demonstrates 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 analog, 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 a 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. |
format | Online Article Text |
id | pubmed-10609797 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-106097972023-10-28 Multifunctional Properties of BMAP-18 and Its Aliphatic Analog against Drug-Resistant Bacteria Jahan, Ishrat Kumar, Sukumar Dinesh Shin, Song Yub Lee, Chul Won Shin, Sung-Heui Yang, Sungtae Pharmaceuticals (Basel) Article BMAP-18, derived from the N-terminal region of bovine myeloid antimicrobial peptide BMAP-27, demonstrates 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 analog, 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 a 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. MDPI 2023-09-25 /pmc/articles/PMC10609797/ /pubmed/37895827 http://dx.doi.org/10.3390/ph16101356 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Jahan, Ishrat Kumar, Sukumar Dinesh Shin, Song Yub Lee, Chul Won Shin, Sung-Heui Yang, Sungtae Multifunctional Properties of BMAP-18 and Its Aliphatic Analog against Drug-Resistant Bacteria |
title | Multifunctional Properties of BMAP-18 and Its Aliphatic Analog against Drug-Resistant Bacteria |
title_full | Multifunctional Properties of BMAP-18 and Its Aliphatic Analog against Drug-Resistant Bacteria |
title_fullStr | Multifunctional Properties of BMAP-18 and Its Aliphatic Analog against Drug-Resistant Bacteria |
title_full_unstemmed | Multifunctional Properties of BMAP-18 and Its Aliphatic Analog against Drug-Resistant Bacteria |
title_short | Multifunctional Properties of BMAP-18 and Its Aliphatic Analog against Drug-Resistant Bacteria |
title_sort | multifunctional properties of bmap-18 and its aliphatic analog against drug-resistant bacteria |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10609797/ https://www.ncbi.nlm.nih.gov/pubmed/37895827 http://dx.doi.org/10.3390/ph16101356 |
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