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Cherniavskyi, Y.K.* ; Oliva, R.* ; Stellato, M.* ; Del Vecchio, P.* ; Galdiero, S.* ; Falanga, A.* ; Dames, S.A. ; Tieleman, D.P.*

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

Biochim. Biophys. Acta-Biomembr. 1866:184272 (2024)

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Free by publisher: Publ. Version/Full Text online available 01/2025

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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.

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Publication type Article: Journal article

Document type Scientific Article

Corresponding Author

Keywords Antimicrobial Peptides ; Bicelle ; Cd ; Liposome ; Membrane Mimetic ; Micelle ; Nmr ; Peptide Lipid Interactions ; Peptide Membrane Interactions ; Suv; Particle Mesh Ewald; Fatc Domain; Lipid-bilayers; Nmr; Antibacterial; Simulations; Rapamycin; Anchor; Target

ISSN (print) / ISBN 0005-2736

e-ISSN 1879-2642

Journal Biochimica et Biophysica Acta - Biomembranes

Quellenangaben Volume: 1866, Issue: 3, Article Number: 184272

Publisher Elsevier

Publishing Place Radarweg 29, 1043 Nx Amsterdam, Netherlands

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) Institute of Structural Biology (STB)

Grants Italian MUR
Canada Foundation
Canada Research Chairs program
Natural Sciences and Engineering Research Council (Canada)
Helmholtz portfolio theme 'metabolic dysfunction and common disease' of the Helmholtz Zentrum Muenchen
Technische Universitat Munchen (TUM) diversity and talent management office by a Laura-Bassi Award
German Research Foundation