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Charge of a transmembrane peptide alters its interaction with lipid membranes.
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SYSNO ASEP 0582992 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, Garima Chand Nakul (UFCH-W)
Uday, Arunima (UFCH-W)
Cebecauer, Marek (UFCH-W) RID, ORCID, SAI
Roos, W. H. (NL)
Cwiklik, Lukasz (UFCH-W) RID, ORCID
Hof, Martin (UFCH-W) RID, ORCID
Jurkiewicz, Piotr (UFCH-W) RID, ORCID
Melcrová, Adéla (UFCH-W)Source Title Colloids and Surfaces B-Biointerfaces. - : Elsevier - ISSN 0927-7765
Roč. 235, MAR 2024 (2024), s. 113765Number of pages 10 s. Language eng - English Country NL - Netherlands Keywords integral membrane protein ; FRET-GP ; AFM imaging Subject RIV CF - Physical ; Theoretical Chemistry OECD category Physical chemistry R&D Projects GX19-26854X GA ČR - Czech Science Foundation (CSF) Method of publishing Open access Institutional support UFCH-W - RVO:61388955 UT WOS 38309153 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 J. Heyrovsky Institute of Physical Chemistry Contact Michaela Knapová, michaela.knapova@jh-inst.cas.cz, Tel.: 266 053 196 Year of Publishing 2025 Electronic address https://hdl.handle.net/11104/0351018
Number of the records: 1