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 15N 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 15N-observed 31P-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. © 2022 The Author(s). Published by Elsevier Inc.

Keywords

Peptides, Lipids, Bacteria, Nucleic acids, Membranes, Salts, Antimicrobial agents, Antibiotics

Citation

Separovic, F., Hofferek, V., Duff, A. P., McConville, M. J., & Sani, M.-A. (2022). In-cell DNP NMR reveals multiple targeting effect of antimicrobial peptide. Journal of Structural Biology: X, 6, 100074. doi:10.1016/j.yjsbx.2022.100074

URI

https://doi.org/10.1016/j.yjsbx.2022.100074
https://apo.ansto.gov.au/handle/10238/16125

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