Rational drug design: Binding free energy differences of carbonic anhydrase inhibitors

M.C. Menziani; C.A. Reynolds; W.G. Richards

doi:10.1039/C39890000853

Rational drug design: Binding free energy differences of carbonic anhydrase inhibitors

M.C. Menziani
, C.A. Reynolds
, W.G. Richards

University of Oxford

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

13 Citations (Scopus)

Abstract

The free energy perturbation method has been applied to calculate the binding energy of sulphonamide inhibitors to carbonic anhydrase; the agreement with experiment gives further evidence for the reliability of this method even for anionic inhibitors and supports its use in drug design.

Original language	English
Pages (from-to)	853-855
Number of pages	3
Journal	Journal of the Chemical Society, Chemical Communications
Volume	13
DOIs	https://doi.org/10.1039/C39890000853
Publication status	Published - 1989
Externally published	Yes

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title = "Rational drug design: Binding free energy differences of carbonic anhydrase inhibitors",

abstract = "The free energy perturbation method has been applied to calculate the binding energy of sulphonamide inhibitors to carbonic anhydrase; the agreement with experiment gives further evidence for the reliability of this method even for anionic inhibitors and supports its use in drug design.",

author = "M.C. Menziani and C.A. Reynolds and W.G. Richards",

year = "1989",

doi = "10.1039/C39890000853",

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journal = "Journal of the Chemical Society, Chemical Communications",

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T2 - Binding free energy differences of carbonic anhydrase inhibitors

AU - Menziani, M.C.

AU - Reynolds, C.A.

AU - Richards, W.G.

PY - 1989

Y1 - 1989

N2 - The free energy perturbation method has been applied to calculate the binding energy of sulphonamide inhibitors to carbonic anhydrase; the agreement with experiment gives further evidence for the reliability of this method even for anionic inhibitors and supports its use in drug design.

AB - The free energy perturbation method has been applied to calculate the binding energy of sulphonamide inhibitors to carbonic anhydrase; the agreement with experiment gives further evidence for the reliability of this method even for anionic inhibitors and supports its use in drug design.

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U2 - 10.1039/C39890000853

DO - 10.1039/C39890000853

M3 - Article

SN - 1364-548X

VL - 13

SP - 853

EP - 855

JO - Journal of the Chemical Society, Chemical Communications

JF - Journal of the Chemical Society, Chemical Communications

ER -

Rational drug design: Binding free energy differences of carbonic anhydrase inhibitors

Abstract

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