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- W1979228034 abstract "The fusion peptide (FP) of the human immunodeficiency virus (HIV) is found on N-terminus of the viral envelope glycoprotein gp41 and is believed to play an important role in the virus entry process. In order to understand the immediate effect of this peptide on the cell membrane we have studied the influence of the synthetic fusion peptide residue FP-23 on the mechanical properties of model lipid bilayers. For this purpose, giant unilamellar vesicles (GUV) were prepared by electroformation from the unsaturated lipid dioleoylphosphatidylcholine mixed in various ratios with the fusion peptide. The bending stiffness of the vesicles was measured with two different methods: fluctuation analysis and aspiration with micropipettes. The data obtained from both of these approaches show that the bending stiffness of the membrane decreases gradually with increasing the concentration of the fusion peptide in the bilayer. Even low concentrations of only a few mol % FP-23 are sufficient to decrease the bending stiffness of the lipid bilayer by more than a factor of two. This observation is in agreement with previous results obtained with X-ray scattering on stacked lipid layers; see Tristram-Nagle and Nagle, Biophys. J. 93: 2048 (2007). Ongoing research is carried out to investigate the effect of FP-23 on the spontaneous fusion of GUVs." @default.
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- W1979228034 date "2010-01-01" @default.
- W1979228034 modified "2023-09-30" @default.
- W1979228034 title "HIV Fusion Peptides Significantly Soften Lipid Bilayers" @default.
- W1979228034 doi "https://doi.org/10.1016/j.bpj.2009.12.1525" @default.
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