Genome-Driven Discovery of Anti-MDR Bacterial Heptapeptides from a Cold-Seep-Derived Strain.
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| Formato: | Artículo científico |
| Lenguaje: | en |
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Molecules (Basel, Switzerland)
2026
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| _version_ | 1868266084897914881 |
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| author | Li, Hongcheng Cheng, Yongmeng Xing, Kaishuai Li, Wenli Xiao, Fei |
| author_facet | Li, Hongcheng Cheng, Yongmeng Xing, Kaishuai Li, Wenli Xiao, Fei Li, Hongcheng Cheng, Yongmeng Xing, Kaishuai Li, Wenli Xiao, Fei |
| collection | PubMed - marine biology |
| contents | Genome-Driven Discovery of Anti-MDR Bacterial Heptapeptides from a Cold-Seep-Derived Strain. Li, Hongcheng Cheng, Yongmeng Xing, Kaishuai Li, Wenli Xiao, Fei Anti-Bacterial Agents Microbial Sensitivity Tests Genome, Bacterial Drug Resistance, Multiple, Bacterial Bacillus Staphylococcus aureus Oligopeptides Structure-Activity Relationship Multigene Family Antimicrobial Peptides With the increasing emergence of multidrug-resistant (MDR) bacteria, there is an urgent need to discover new antibiotics. In this study, genome mining coupled with anti-bacterial assay guided the targeted isolation of two new heptapeptides nobilamide Q3 () and R3 (). These compounds were identified as new stereoisomers of the known scaffold A-3302-B (). The structures of these compounds were elucidated through a combination of MS, NMR spectroscopy and Marfey's analysis. Anti-MDR bacterial assays showed that compounds and exhibited effective growth inhibition against the Gram-positive MDR bacterial strain CCARM 3090 with MIC values of 3.25-6.5 μg/mL. Notably, our study reveals stereochemistry-dependent differences in their antibacterial activities, providing new insights into the structure-activity relationship of this class of peptides. Finally, an analysis of the biosynthetic gene cluster responsible for their production was conducted. This study underscores the significance of exploring cold-seep environments as a reservoir for discovering new antibiotics and provides a structural starting point for the future optimization of antimicrobial peptides. |
| format | Artículo científico |
| id | pubmed_41683524 |
| institution | PubMed |
| language | en |
| publishDate | 2026 |
| publisher | Molecules (Basel, Switzerland) |
| record_format | pubmed |
| spellingShingle | Genome-Driven Discovery of Anti-MDR Bacterial Heptapeptides from a Cold-Seep-Derived Strain. Li, Hongcheng Cheng, Yongmeng Xing, Kaishuai Li, Wenli Xiao, Fei Anti-Bacterial Agents Microbial Sensitivity Tests Genome, Bacterial Drug Resistance, Multiple, Bacterial Bacillus Staphylococcus aureus Oligopeptides Structure-Activity Relationship Multigene Family Antimicrobial Peptides Genome-Driven Discovery of Anti-MDR Bacterial Heptapeptides from a Cold-Seep-Derived Strain. Li, Hongcheng Cheng, Yongmeng Xing, Kaishuai Li, Wenli Xiao, Fei Anti-Bacterial Agents Microbial Sensitivity Tests Genome, Bacterial Drug Resistance, Multiple, Bacterial Bacillus Staphylococcus aureus Oligopeptides Structure-Activity Relationship Multigene Family Antimicrobial Peptides With the increasing emergence of multidrug-resistant (MDR) bacteria, there is an urgent need to discover new antibiotics. In this study, genome mining coupled with anti-bacterial assay guided the targeted isolation of two new heptapeptides nobilamide Q3 () and R3 (). These compounds were identified as new stereoisomers of the known scaffold A-3302-B (). The structures of these compounds were elucidated through a combination of MS, NMR spectroscopy and Marfey's analysis. Anti-MDR bacterial assays showed that compounds and exhibited effective growth inhibition against the Gram-positive MDR bacterial strain CCARM 3090 with MIC values of 3.25-6.5 μg/mL. Notably, our study reveals stereochemistry-dependent differences in their antibacterial activities, providing new insights into the structure-activity relationship of this class of peptides. Finally, an analysis of the biosynthetic gene cluster responsible for their production was conducted. This study underscores the significance of exploring cold-seep environments as a reservoir for discovering new antibiotics and provides a structural starting point for the future optimization of antimicrobial peptides. |
| title | Genome-Driven Discovery of Anti-MDR Bacterial Heptapeptides from a Cold-Seep-Derived Strain. |
| topic | Anti-Bacterial Agents Microbial Sensitivity Tests Genome, Bacterial Drug Resistance, Multiple, Bacterial Bacillus Staphylococcus aureus Oligopeptides Structure-Activity Relationship Multigene Family Antimicrobial Peptides |
| url | https://pubmed.ncbi.nlm.nih.gov/41683524/ |