Antiviral drug design: computational analyses of the effects of the L100I mutation for HIV-RT on the binding of NNRTIs.

D. P. Wang; R. C. Rizzo; J. Tirado-Rives; W. L. Jorgensen

doi:10.1016/S0960-894X(01)00510-8

Antiviral drug design: computational analyses of the effects of the L100I mutation for HIV-RT on the binding of NNRTIs.

D. P. Wang
, R. C. Rizzo
, J. Tirado-Rives
, W. L. Jorgensen

Applied Mathematics and Statistics

Stony Brook University

Yale University

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

44 Scopus citations

Abstract

Monte Carlo/free energy perturbation (MC/FEP) calculations were used to evaluate the binding free energy change for HIV-RT/inhibitor complexes upon L100I mutation. Inhibitor size and flexibility adjacent to hydrogen-bonding sites are evident as important considerations for antiviral drug design.

Original language	English
Pages (from-to)	2799-2802
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	11
Issue number	21
DOIs	https://doi.org/10.1016/S0960-894X(01)00510-8
State	Published - Nov 5 2001

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10.1016/S0960-894X(01)00510-8

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title = "Antiviral drug design: computational analyses of the effects of the L100I mutation for HIV-RT on the binding of NNRTIs.",

abstract = "Monte Carlo/free energy perturbation (MC/FEP) calculations were used to evaluate the binding free energy change for HIV-RT/inhibitor complexes upon L100I mutation. Inhibitor size and flexibility adjacent to hydrogen-bonding sites are evident as important considerations for antiviral drug design.",

author = "Wang, \{D. P.\} and Rizzo, \{R. C.\} and J. Tirado-Rives and Jorgensen, \{W. L.\}",

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T2 - computational analyses of the effects of the L100I mutation for HIV-RT on the binding of NNRTIs.

AU - Wang, D. P.

AU - Rizzo, R. C.

AU - Tirado-Rives, J.

AU - Jorgensen, W. L.

PY - 2001/11/5

Y1 - 2001/11/5

N2 - Monte Carlo/free energy perturbation (MC/FEP) calculations were used to evaluate the binding free energy change for HIV-RT/inhibitor complexes upon L100I mutation. Inhibitor size and flexibility adjacent to hydrogen-bonding sites are evident as important considerations for antiviral drug design.

AB - Monte Carlo/free energy perturbation (MC/FEP) calculations were used to evaluate the binding free energy change for HIV-RT/inhibitor complexes upon L100I mutation. Inhibitor size and flexibility adjacent to hydrogen-bonding sites are evident as important considerations for antiviral drug design.

UR - https://www.scopus.com/pages/publications/0035814027

U2 - 10.1016/S0960-894X(01)00510-8

DO - 10.1016/S0960-894X(01)00510-8

M3 - Article

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SN - 0960-894X

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JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

IS - 21

ER -

Antiviral drug design: computational analyses of the effects of the L100I mutation for HIV-RT on the binding of NNRTIs.

Abstract

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