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...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-09-01
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| Series: | Pharmaceuticals |
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| Online Access: | https://www.mdpi.com/1424-8247/16/10/1356 |
| _version_ | 1797572613831131136 |
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| author | Ishrat Jahan Sukumar Dinesh Kumar Song Yub Shin Chul Won Lee Sung-Heui Shin Sungtae Yang |
| author_facet | Ishrat Jahan Sukumar Dinesh Kumar Song Yub Shin Chul Won Lee Sung-Heui Shin Sungtae Yang |
| author_sort | Ishrat Jahan |
| collection | DOAJ |
| 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 <i>Staphylococcus aureus</i> (MRSA) and multidrug-resistant <i>Pseudomonas aeruginosa</i> (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. |
| first_indexed | 2024-03-10T20:58:28Z |
| format | Article |
| id | doaj.art-30cfcbc6526f40d4ad8a0c7faccb2563 |
| institution | Directory Open Access Journal |
| issn | 1424-8247 |
| language | English |
| last_indexed | 2024-03-10T20:58:28Z |
| publishDate | 2023-09-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Pharmaceuticals |
| spelling | doaj.art-30cfcbc6526f40d4ad8a0c7faccb25632023-11-19T17:41:18ZengMDPI AGPharmaceuticals1424-82472023-09-011610135610.3390/ph16101356Multifunctional Properties of BMAP-18 and Its Aliphatic Analog against Drug-Resistant BacteriaIshrat Jahan0Sukumar Dinesh Kumar1Song Yub Shin2Chul Won Lee3Sung-Heui Shin4Sungtae Yang5Department of Biomedical Sciences, School of Medicine, Chosun University, Gwangju 61452, Republic of KoreaDepartment of Cellular and Molecular Medicine, School of Medicine, Chosun University, Gwangju 61452, Republic of KoreaDepartment of Cellular and Molecular Medicine, School of Medicine, Chosun University, Gwangju 61452, Republic of KoreaDepartment of Chemistry, Chonnam National University, Gwangju 61186, Republic of KoreaDepartment of Cellular and Molecular Medicine, School of Medicine, Chosun University, Gwangju 61452, Republic of KoreaDepartment of Microbiology, School of Medicine, Chosun University, Gwangju 61452, Republic of KoreaBMAP-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 <i>Staphylococcus aureus</i> (MRSA) and multidrug-resistant <i>Pseudomonas aeruginosa</i> (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.https://www.mdpi.com/1424-8247/16/10/1356antimicrobial peptidedrug-resistant bacteriacathelicidinmultifunctionaromatic and aliphatic residue |
| spellingShingle | Ishrat Jahan Sukumar Dinesh Kumar Song Yub Shin Chul Won Lee Sung-Heui Shin Sungtae Yang Multifunctional Properties of BMAP-18 and Its Aliphatic Analog against Drug-Resistant Bacteria Pharmaceuticals antimicrobial peptide drug-resistant bacteria cathelicidin multifunction aromatic and aliphatic residue |
| 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 | antimicrobial peptide drug-resistant bacteria cathelicidin multifunction aromatic and aliphatic residue |
| url | https://www.mdpi.com/1424-8247/16/10/1356 |
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