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In-cell DNP NMR reveals multiple targeting effect of antimicrobial peptide

Dynamic nuclear polarization NMR spectroscopy was used to investigate the effect of the antimicrobial peptide (AMP) maculatin 1.1 on E. coli cells. The enhanced (15)N NMR signals from nucleic acids, proteins and lipids identified a number of unanticipated physiological responses to peptide stress, r...

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Detalles Bibliográficos
Autores principales: Separovic, Frances, Hofferek, Vinzenz, Duff, Anthony P., McConville, Malcom J., Sani, Marc-Antoine
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9486116/
https://www.ncbi.nlm.nih.gov/pubmed/36147732
http://dx.doi.org/10.1016/j.yjsbx.2022.100074
Descripción
Sumario:Dynamic nuclear polarization NMR spectroscopy was used to investigate the effect of the antimicrobial peptide (AMP) maculatin 1.1 on E. coli cells. The enhanced (15)N NMR signals from nucleic acids, proteins and lipids identified a number of unanticipated physiological responses to peptide stress, revealing that membrane-active AMPs can have a multi-target impact on E. coli cells. DNP-enhanced (15)N-observed (31)P-dephased REDOR NMR allowed monitoring how Mac1 induced DNA condensation and prevented intermolecular salt bridges between the main E. coli lipid phosphatidylethanolamine (PE) molecules. The latter was supported by similar results obtained using E. coli PE lipid systems. Overall, the ability to monitor the action of antimicrobial peptides in situ will provide greater insight into their mode of action.