HIV-1 Tat membrane interactions probed using X-ray and neutron scattering, CD spectroscopy and MD simulations.

Autor:	Akabori K; Department of Physics, Carnegie Mellon University, 5000 Forbes Avenue, Pittsburgh, PA, United States., Huang K; Department of Physics, Rensselaer Polytechnic Institute, 110 Eighth Street, Troy, NY 12180, United States., Treece BW; Department of Physics, Carnegie Mellon University, 5000 Forbes Avenue, Pittsburgh, PA, United States., Jablin MS; Department of Physics, Carnegie Mellon University, 5000 Forbes Avenue, Pittsburgh, PA, United States., Maranville B; NIST Center for Neutron Research, 100 Bureau Drive, Stop 6102, Gaithersburg, MD 20899, United States., Woll A; CHESS, Cornell University, 161 Synchrotron Drive, Ithaca, NY 14853, United States., Nagle JF; Department of Physics, Carnegie Mellon University, 5000 Forbes Avenue, Pittsburgh, PA, United States., Garcia AE; Department of Physics, Rensselaer Polytechnic Institute, 110 Eighth Street, Troy, NY 12180, United States., Tristram-Nagle S; Department of Physics, Carnegie Mellon University, 5000 Forbes Avenue, Pittsburgh, PA, United States. Electronic address: stn@cmu.edu.
Jazyk:	angličtina
Zdroj:	Biochimica et biophysica acta [Biochim Biophys Acta] 2014 Dec; Vol. 1838 (12), pp. 3078-87. Date of Electronic Publication: 2014 Aug 19.
DOI:	10.1016/j.bbamem.2014.08.014
Abstrakt:	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. (Copyright © 2014 Elsevier B.V. All rights reserved.)
Databáze:	MEDLINE
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