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• W2172180260 endingPage "3087" @default.
• W2172180260 startingPage "3078" @default.
• W2172180260 abstract "We report the effect on lipid bilayers of the Tat peptide Y47GRKKRRQRRR57 from the HIV-1 virus transactivator of translation (Tat) protein. Synergistic use of low-angle X-ray scattering (LAXS) and atomistic molecular dynamic simulations (MD) indicate Tat peptide binding to neutral dioleoylphosphocholine (DOPC) lipid headgroups. This binding induced the local lipid phosphate groups to move 3Å closer to the center of the bilayer. Many of the positively charged guanidinium components of the arginines were as close to the center of the bilayer as the locally thinned lipid phosphate groups. LAXS data for DOPC, DOPC/dioleoylphosphoethanolamine (DOPE), DOPC/dioleoylphosphoserine (DOPS), and a mimic of the nuclear membrane gave similar results. Generally, the Tat peptide decreased the bilayer bending modulus KC and increased the area/lipid. Further indications that Tat softens a membrane, thereby facilitating translocation, were provided by wide-angle X-ray scattering (WAXS) and neutron scattering. CD spectroscopy was also applied to further characterize Tat/membrane interactions. Although a mechanism for translation remains obscure, this study suggests that the peptide/lipid interaction makes the Tat peptide poised to translocate from the headgroup region." @default.
• W2172180260 created "2016-06-24" @default.
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• W2172180260 creator A5089866741 @default.
• W2172180260 date "2014-12-01" @default.
• W2172180260 modified "2023-10-02" @default.
• W2172180260 title "HIV-1 Tat membrane interactions probed using X-ray and neutron scattering, CD spectroscopy and MD simulations" @default.
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• W2172180260 doi "https://doi.org/10.1016/j.bbamem.2014.08.014" @default.
• W2172180260 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4610132" @default.
• W2172180260 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25148702" @default.
• W2172180260 hasPublicationYear "2014" @default.
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