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Structural study of a new HIV-1 entry inhibitor and interaction with the HIV-1 fusion peptide in dodecylphosphocholine micelles.

Structural study of a new HIV-1 entry inhibitor and interaction with the HIV-1 fusion peptide in dodecylphosphocholine micelles.
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Pérez Y, Gómara MJ, Yuste E, Gómez-Gutierrez P, Pérez JJ, Haro I,


Pérez Y, Gómara MJ, Yuste E, Gómez-Gutierrez P, Pérez JJ, Haro I, (click to view)

Pérez Y, Gómara MJ, Yuste E, Gómez-Gutierrez P, Pérez JJ, Haro I,

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Chemistry (Weinheim an der Bergstrasse, Germany) 2017 07 05() doi 10.1002/chem.201702531

Abstract

Previous studies support the hypothesis that the envelope GB virus C E1 protein interferes HIV-1 entry and a peptide, derived from the region (139-156) of this protein, has defined as a novel HIV-1 entry inhibitor. In this work, we firstly focus on the characterization of the peptide structural features which are determinant for its anti-HIV-1 activity and secondly, on the study of its interaction of with the proposed viral target (the HIV-1 fusion peptide). We report the peptide structure determined by NMR spectroscopy in DPC micelles solved using restrained molecular dynamics calculations. The acquisition of different NMR experiments in DPC micelles (peptide-peptide titration, diffusion NMR and addition of paramagnetic relaxation agents) allows the proposal of an inhibition mechanism. We conclude that an 18-mer peptide from non-pathogenic E1 GBV-C protein, with a helix-turn-helix structure, inhibits HIV-1 by binding to the HIV-1 fusion peptide at membrane level interfering with those domains in HIV-1 that are critical for stabilizing the six-helix bundle formation in a membranous environment.

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