دورية أكاديمية
Charge of a transmembrane peptide alters its interaction with lipid membranes
| العنوان: | Charge of a transmembrane peptide alters its interaction with lipid membranes |
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| المؤلفون: | Thakur, Garima C.N., Uday, Arunima, Cebecauer, Marek, Roos, Wouter H., Cwiklik, Lukasz, Hof, Martin, Jurkiewicz, Piotr, Melcrová, Adéla |
| المصدر: | Thakur , G C N , Uday , A , Cebecauer , M , Roos , W H , Cwiklik , L , Hof , M , Jurkiewicz , P & Melcrová , A 2024 , ' Charge of a transmembrane peptide alters its interaction with lipid membranes ' , Colloids and Surfaces B: Biointerfaces , vol. 235 , 113765 . https://doi.org/10.1016/j.colsurfb.2024.113765Test |
| سنة النشر: | 2024 |
| المجموعة: | University of Groningen research database |
| مصطلحات موضوعية: | AFM imaging, AFM nanoindentation, FRET-GP, Integral membrane protein, MD simulation |
| الوصف: | 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. |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | application/pdf |
| اللغة: | English |
| العلاقة: | https://research.rug.nl/en/publications/089a102f-22d5-4add-bafb-4ce9c61dc659Test |
| DOI: | 10.1016/j.colsurfb.2024.113765 |
| الإتاحة: | https://doi.org/10.1016/j.colsurfb.2024.113765Test https://hdl.handle.net/11370/089a102f-22d5-4add-bafb-4ce9c61dc659Test https://research.rug.nl/en/publications/089a102f-22d5-4add-bafb-4ce9c61dc659Test https://pure.rug.nl/ws/files/932119624/1-s2.0-S0927776524000237-main.pdfTest http://www.scopus.com/inward/record.url?scp=85184063912&partnerID=8YFLogxKTest |
| حقوق: | info:eu-repo/semantics/openAccess |
| رقم الانضمام: | edsbas.6D511019 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1016/j.colsurfb.2024.113765 |
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