Structural characterization of the antimicrobial peptides myxinidin and WMR in bacterial membrane mimetic micelles and bicelles.

Autor: Cherniavskyi YK; Department of Biological Sciences and Centre for Molecular Simulation, University of Calgary, 2500 University Drive NW, Calgary, Alberta T2N 1N4, Canada., Oliva R; Department of Chemical Sciences, University of Naples 'Federico II', via Cintia, 80126 Naples, Italy., Stellato M; Department of Chemical Sciences, University of Naples 'Federico II', via Cintia, 80126 Naples, Italy., Del Vecchio P; Department of Chemical Sciences, University of Naples 'Federico II', via Cintia, 80126 Naples, Italy., Galdiero S; Department of Pharmacy, University of Naples 'Federico II', Via Domenico Montesano 49, 80131 Naples, Italy., Falanga A; Department of Agricultural Science, University of Naples 'Federico II', Via dell' Università 100, 80055 Portici, Naples, Italy., Dames SA; Chair of Biomolecular NMR Spectroscopy, Department of Chemistry, Technische Universität München, Lichtenbergstr. 4, 85747 Garching, Germany; Hausdorff Center for Mathematics, University of Bonn, Endenicher Allee 62, 53115 Bonn, Germany; Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstr. 1, 85764 Neuherberg, Germany. Electronic address: sonja.dames@tum.de., Tieleman DP; Department of Biological Sciences and Centre for Molecular Simulation, University of Calgary, 2500 University Drive NW, Calgary, Alberta T2N 1N4, Canada. Electronic address: tieleman@ucalgary.ca.
Jazyk: angličtina
Zdroj: Biochimica et biophysica acta. Biomembranes [Biochim Biophys Acta Biomembr] 2024 Mar; Vol. 1866 (3), pp. 184272. Date of Electronic Publication: 2024 Jan 09.
DOI: 10.1016/j.bbamem.2024.184272
Abstrakt: Antimicrobial peptides are a promising class of potential antibiotics that interact selectively with negatively charged lipid bilayers. This paper presents the structural characterization of the antimicrobial peptides myxinidin and WMR associated with bacterial membrane mimetic micelles and bicelles by NMR, CD spectroscopy, and molecular dynamics simulations. Both peptides adopt a different conformation in the lipidic environment than in aqueous solution. The location of the peptides in micelles and bicelles has been studied by paramagnetic relaxation enhancement experiments with paramagnetic tagged 5- and 16-doxyl stearic acid (5-/16-SASL). Molecular dynamics simulations of multiple copies of the peptides were used to obtain an atomic level of detail on membrane-peptide and peptide-peptide interactions. Our results highlight an essential role of the negatively charged membrane mimetic in the structural stability of both myxinidin and WMR. The peptides localize predominantly in the membrane's headgroup region and have a noticeable membrane thinning effect on the overall bilayer structure. Myxinidin and WMR show a different tendency to self-aggregate, which is also influenced by the membrane composition (DOPE/DOPG versus DOPE/DOPG/CL) and can be related to the previously observed difference in the ability of the peptides to disrupt different types of model membranes.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024. Published by Elsevier B.V.)
Databáze: MEDLINE
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