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- W2034644942 abstract "The HIV-1 envelope glycoprotein 41 (gp41) undergoes large-scale conformational changes in order to induce the fusion of the virus and cell membranes. Thus, we investigated a possible structure transit at the air-water interface for the tryptophan-rich peptide of gp41 (gp41W). The synthetic peptide (KWASLWNWFNITNWLWYIK), corresponding to gp41W, shows interfacial properties on pure water and Tris buffer at pH 8.5. Isotherm measurements and Brewster angle microscopy (BAM) imaging showed that the behavior of the peptide monolayer was dependent on the subphase composition. A homogenous film was formed on buffer during the peptide monolayer compression, while the appearance of condensed domains on pure water could indicate the oligomerization of gp41W during the surface pressure increase. Polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS) showed that, whatever the subphase, gp41W adopts an α-helix structure at the air-water interface and does not transit for any other structure even at high surface pressures." @default.
- W2034644942 created "2016-06-24" @default.
- W2034644942 creator A5014426060 @default.
- W2034644942 creator A5024740475 @default.
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- W2034644942 date "2010-12-01" @default.
- W2034644942 modified "2023-10-12" @default.
- W2034644942 title "Interfacial properties and structure stability of the gp41 tryptophan-rich peptide from HIV-1" @default.
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- W2034644942 doi "https://doi.org/10.1016/j.jcis.2010.08.075" @default.
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