@article{9a9274b0c7344ed5b0195dc33f15e6a1,
title = "Interaction of amiloride and one of its derivatives with Vpu from HIV-1: A molecular dynamics simulation",
abstract = "Vpu is an 81-residue membrane protein, with a single transmembrane segment that is encoded by HIV-1 and is involved in the enhancement of virion release via formation of an ion channel. Cyclohexamethylene amiloride (Hma) has been shown to inhibit ion channel activity. In the present 12-ns simulation study a putative binding site of Hma blockers in a pentameric model bundle built of parallel aligned helices of the first 32 residues of Vpu was found near Ser-23. Hma orientates along the channel axis with its alkyl ring pointing inside the pore, which leads to a blockage of the pore.",
keywords = "Drug-protein interaction, HIV-1, Molecular dynamics simulation, Viral ion channel, Vpu",
author = "V. Lemaitre and R. Ali and Kim, {C. G.} and A. Watts and Fischer, {W. B.}",
note = "Funding Information: W.B.F. thanks the E.P. Abraham Research Fund for financial support of this work. The Engineering and Physical Science Research Council (EPSRC), Medical Research Council (MRC), the Biological Science Research Council, the Bionanotechnology IRC and CJ Corporation (for financial support to C.G.K.) are all acknowledged for grant support to A.W. We thank CCLRC-RAL for computer facilities and service. ",
year = "2004",
month = apr,
day = "9",
doi = "10.1016/S0014-5793(04)00251-0",
language = "English",
volume = "563",
pages = "75--81",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Wiley-Blackwell",
number = "1-3",
}
