Calculations of the electrostatic free energy contributions to the binding free energy of sulfonamides to carbonic anhydrase

Jeffry D. Madura, Yasushi Nakajima, Rodney M. Hamilton, Andrzej Wierzbicki, Arieh Warshel

研究成果: Article査読

19 被引用数 (Scopus)

抄録

The interactions between biologically important enzymes and drugs are of great interest. In order to address some aspects of these interactions we have initiated a program to investigate enzyme-drug interactions. Specifically, the interactions between one of the isozymes of carbonic anhydrase and a family of drugs known as sulfonamides have been studied using computational methods. In particular the electrostatic free energy of binding of carbonic anhydrase II with acetazolamide, methazolamide, p-chlorobenzenesulfonamide, p-aminobenzenesulfonamide and three new compounds (MK1, MK2, and MK3) has been computed using finite-difference Poisson-Boltzmann (FDPB) [1] method and the semimacroscopic version [2, 3] of the protein dipole Langevin dipole (PDLD) method [4]. Both methods, FDPB and PDLD, give similar results for the electrostatic free energy of binding even though different charges and different treatments were used for the protein. The calculated electrostatic binding free energies are in reasonable agreement with the experimental data. The potential and the limitation of electrostatic models for studies of binding energies are discussed.

本文言語English
ページ(範囲)131-138
ページ数8
ジャーナルStructural Chemistry
7
2
DOI
出版ステータスPublished - 1996 4
外部発表はい

ASJC Scopus subject areas

  • Condensed Matter Physics
  • Physical and Theoretical Chemistry

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