Interaction of amiloride and one of its derivatives with Vpu from HIV-1: A molecular dynamics simulation

V. Lemaitre; R. Ali; C. G. Kim; A. Watts; W. B. Fischer

doi:10.1016/S0014-5793(04)00251-0

Interaction of amiloride and one of its derivatives with Vpu from HIV-1: A molecular dynamics simulation

V. Lemaitre, R. Ali, C. G. Kim, A. Watts, W. B. Fischer^*

^*Corresponding author for this work

Institute of Biophotonics

Research output: Contribution to journal › Article › peer-review

30 Scopus citations

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.

Original language	English
Pages (from-to)	75-81
Number of pages	7
Journal	FEBS Letters
Volume	563
Issue number	1-3
DOIs	https://doi.org/10.1016/S0014-5793(04)00251-0
State	Published - 9 Apr 2004

Keywords

Drug-protein interaction
HIV-1
Molecular dynamics simulation
Viral ion channel
Vpu

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/S0014-5793(04)00251-0

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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. ",

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doi = "10.1016/S0014-5793(04)00251-0",

language = "English",

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T2 - A molecular dynamics simulation

AU - Lemaitre, V.

AU - Ali, R.

AU - Kim, C. G.

AU - Watts, A.

AU - Fischer, W. B.

N1 - 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.

PY - 2004/4/9

Y1 - 2004/4/9

N2 - 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.

AB - 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.

KW - Drug-protein interaction

KW - HIV-1

KW - Molecular dynamics simulation

KW - Viral ion channel

KW - Vpu

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U2 - 10.1016/S0014-5793(04)00251-0

DO - 10.1016/S0014-5793(04)00251-0

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AN - SCOPUS:1842788183

SN - 0014-5793

VL - 563

SP - 75

EP - 81

JO - FEBS Letters

JF - FEBS Letters

IS - 1-3

ER -

Interaction of amiloride and one of its derivatives with Vpu from HIV-1: A molecular dynamics simulation

Abstract

Keywords

UN SDGs

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