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Vpu is an 81-amino-acid auxiliary protein of the genome of HIV-1. It is proposed that one of its roles is to enhance particle release by self-assembling to form water-filled channels enabling the flux of ions at the site of the plasma membrane of the infected cell. Hexamethylene amiloride has been shown to block Vpu channel activity when the protein is reconstituted into lipid bilayers. In a docking approach with monomeric, pentameric and hexameric bundle models of Vpu corresponding to the transmembrane part of the protein, a putative binding site of hexamethylene amiloride is proposed and is compared with the site for the nonpotent amiloride. The binding mode for both ligands is achieved by optimizing hydrogen bond interactions with serines. Binding energies and binding constants are the lowest for protonated hexamethylene amiloride in the pentameric bundle.

Original publication

DOI

10.1007/s00216-006-0832-4

Type

Journal article

Journal

Anal Bioanal Chem

Publication Date

12/2006

Volume

386

Pages

2213 - 2217

Keywords

Amiloride, Binding Sites, HIV-1, Human Immunodeficiency Virus Proteins, Hydrogen Bonding, Ligands, Models, Molecular, Protein Binding, Protein Structure, Tertiary, Viral Regulatory and Accessory Proteins