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Charge of a transmembrane peptide alters its interaction with lipid membranes.
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SYSNO ASEP 0582943 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Charge of a transmembrane peptide alters its interaction with lipid membranes. Author(s) Thakur, G. C. N. (CZ)
Uday, A. (CZ)
Cebecauer, M. (CZ)
Roos, W. H. (CZ)
Cwiklik, Lukasz (UOCHB-X) RID, ORCID
Hof, M. (CZ)
Jurkiewicz, P. (CZ)
Melcrová, A. (CZ)Article number 113765 Source Title Colloids and Surfaces B-Biointerfaces. - : Elsevier - ISSN 0927-7765
Roč. 235, March (2024)Number of pages 10 s. Language eng - English Country NL - Netherlands Keywords Integral membrane protein ; FRET-GP ; AFM imaging ; AFM nanoindentation ; MD simulation R&D Projects GX19-26854X GA ČR - Czech Science Foundation (CSF) Method of publishing Open access Institutional support UOCHB-X - RVO:61388963 UT WOS 001179895200001 EID SCOPUS 85184063912 DOI 10.1016/j.colsurfb.2024.113765 Annotation Transmembrane (TM) proteins interact closely with the surrounding membrane lipids. Lipids in the vicinity of TM proteins were reported to have hindered mobility, which has been associated with lipids being caught up in the rough surface of the TM domains. These reports, however, neglect one important factor that largely influences the membrane behavior electrostatics of the TM peptides that are usually positively charged at their cytosolic end. Here, we study on the example of a neutral and a positively charged WALP peptide, how the charge of a TM peptide influences the membrane. We investigate both its dynamics and mechanics by: (i) time dependent fluorescent shift in combination with classical and FRET generalized polarization to evaluate the mobility of lipids at short and long-range distance from the peptide, (ii) atomic force microscopy to observe the mechanical stability of the peptide-containing membranes, and (iii) molecular dynamics simulations to analyze the peptide-lipid interactions. We show that both TM peptides lower lipid mobility in their closest surroundings. The peptides cause lateral heterogeneity in lipid mobility, which in turn prevents free lipid rearrangement and lowers the membrane ability to seal ruptures after mechanical indentations. Introduction of a positive charge to the peptide largely enhances these effects, affecting the whole membrane. We thus highlight that unspecific peptide-lipid interactions, especially the electrostatics, should not be overlooked as they have a great impact on the mechanics and dynamics of the whole membrane. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Year of Publishing 2025 Electronic address https://doi.org/10.1016/j.colsurfb.2024.113765
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