{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["2"],"submitter":["Kumari S"],"pubmed_abstract":["Understanding how non-lipid components of bacteria affect antimicrobial peptide (AMP)-induced membrane disruption is important for a comprehensive understanding of AMP mechanisms and informing AMP-based drug development. This study investigates how lipopolysaccharide (LPS) affects membrane disruption by the AMP MSI-78 and compares the results to the effect of TP2, a cell-penetrating peptide that crosses membrane bilayers without permeabilizing them. We destabilize the LPS layer of <i>Escherichia coli</i> (<i>E. coli</i>) cells via chelation of the stabilizing divalent cations. <sup>2</sup>H NMR spectra of <i>E. coli</i> demonstrate that EDTA concentrations of 2.5 mM and 9.0 mM alone have very minor effects on lipid acyl chain order. Interestingly, we find that <i>E. coli</i> pre-treated with 9.0 mM EDTA before treatment with MSI-78 are more sensitive to AMP-induced acyl chain disruption, indicating that intact LPS reduces MSI-78-induced membrane disruption in <i>E. coli</i>. Surprisingly, we also found that at the level of <sup>2</sup>H_NMR, the peptide-induced acyl chain disruption is similar for MSI-78 and TP2, although MSI-78 permeabilizes the bilayer and TP2 does not. Furthermore, LPS disruption appears to protect the bacteria from TP2, although it sensitizes them to MSI-78."],"journal":["BBA advances"],"pagination":["100057"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10074874"],"repository":["biostudies-literature"],"pubmed_title":["Role of lipopolysaccharide in antimicrobial and cell penetrating peptide membrane interactions probed by deuterium NMR of whole cells."],"pmcid":["PMC10074874"],"pubmed_authors":["Morrow MR","Kumari S","Booth V"],"additional_accession":[]},"is_claimable":false,"name":"Role of lipopolysaccharide in antimicrobial and cell penetrating peptide membrane interactions probed by deuterium NMR of whole cells.","description":"Understanding how non-lipid components of bacteria affect antimicrobial peptide (AMP)-induced membrane disruption is important for a comprehensive understanding of AMP mechanisms and informing AMP-based drug development. This study investigates how lipopolysaccharide (LPS) affects membrane disruption by the AMP MSI-78 and compares the results to the effect of TP2, a cell-penetrating peptide that crosses membrane bilayers without permeabilizing them. We destabilize the LPS layer of <i>Escherichia coli</i> (<i>E. coli</i>) cells via chelation of the stabilizing divalent cations. <sup>2</sup>H NMR spectra of <i>E. coli</i> demonstrate that EDTA concentrations of 2.5 mM and 9.0 mM alone have very minor effects on lipid acyl chain order. Interestingly, we find that <i>E. coli</i> pre-treated with 9.0 mM EDTA before treatment with MSI-78 are more sensitive to AMP-induced acyl chain disruption, indicating that intact LPS reduces MSI-78-induced membrane disruption in <i>E. coli</i>. Surprisingly, we also found that at the level of <sup>2</sup>H_NMR, the peptide-induced acyl chain disruption is similar for MSI-78 and TP2, although MSI-78 permeabilizes the bilayer and TP2 does not. Furthermore, LPS disruption appears to protect the bacteria from TP2, although it sensitizes them to MSI-78.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2025-04-22T01:37:38.737Z","creation":"2025-04-05T20:05:20.094Z"},"accession":"S-EPMC10074874","cross_references":{"pubmed":["37082590"],"doi":["10.1016/j.bbadva.2022.100057"]}}