Three conserved C-terminal residues of influenza fusion peptide alter its behavior at the membrane interface

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• 作者：Remigiusz Worch^a ; ^{remiwo@ifpan.edu.pl} ; Joanna Krupa^a ; Alicja Filipek^a ; ¹ ; Anna Szymaniec^a ; ² ; Piotr Setny^b
• 关键词：Peptide-lipid interactions ; Confocal microscopy ; Lifetime imaging microscopy ; Giant unilamellar vesicles ; Fluorescence ; Influenza virus ; Molecular simulations
• 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：1861
• 期：2
• 页码：97-105
• 全文大小：1348 K
• 卷排序：1861

文摘

Behavior of influenza fusion peptides at the membrane interface depends on its length. Presence of C-terminal W21-Y22-G23 leads to more disorder in the surrounding lipids. Fusogenic activity seems to correlate with transmembrane peptide configuration. Cholesterol-enriched peptide induced domain formation is observed. Novel fusion visualization assay based on FLIM microscopy on GUV is developed.