An ab initio study of di- and trifluorobenzene-benzene complexes as relevant to carbonic anhydrase II-drug interactions

Ab initio calculations at the MP2/6-31G* level have shown that variously substituted di- and trifluorobenzenes form non-covalent complexes with benzene that adopt either aromatic-aromatic or H--F binding, the choice being determined by the pattern of fluorination. The binding energies of these struc...

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Bibliographic Details
Published inJournal of molecular modeling Vol. 10; no. 1; pp. 1 - 5
Main Authors Chandra, Pooja P, Jain, Ahamindra, Sapse, Anne-Marie
Format Journal Article
LanguageEnglish
Published Germany 01.02.2004
Subjects
Benzene Derivatives
Binding Sites
Carbonic Anhydrase II - chemistry
Carbonic Anhydrase II - metabolism
Carbonic Anhydrase Inhibitors - chemistry
Computer Simulation
Fluorobenzenes - chemistry
Hydrocarbons, Aromatic
Models, Chemical
Models, Molecular
Molecular Conformation
Molecular Structure
Protein Binding
Software
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Summary:Ab initio calculations at the MP2/6-31G* level have shown that variously substituted di- and trifluorobenzenes form non-covalent complexes with benzene that adopt either aromatic-aromatic or H--F binding, the choice being determined by the pattern of fluorination. The binding energies of these structures are from 3.4 to 4.5 kcal mol(-1). This range is large enough to account for observed variations in the binding affinity of a library of fluoroaromatic inhibitors of carbonic anhydrase. This enzyme has an aromatic amino acid at a central position in the active site. The diverse modes of binding of the dimers also suggest that aggregates of fluorobenzenes might adopt specified 3-dimensional shapes in the solid state.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:1610-2940
0948-5023
DOI:10.1007/s00894-003-0146-9