title: An ab initio study of di- and trifluorobenzene-benzene complexes as relevant to carbonic anhydrase II-drug interactions.
abstract: 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.
authors.affiliation: Swarthmore College, Swarthmore, PA 19081, USA.
authors.forename: Pooja P
authors.initials: PP
authors.lastname: Chandra
authors.forename: Ahamindra
authors.initials: A
authors.lastname: Jain
authors.forename: Anne-Marie
authors.initials: AM
authors.lastname: Sapse
mesh_terms: D001555:Benzene Derivatives; D001665:Binding Sites; D024402:Carbonic Anhydrase II / Q000737:chemistry* / Q000378:metabolism; D002257:Carbonic Anhydrase Inhibitors / Q000737:chemistry; D003198:Computer Simulation; D005464:Fluorobenzenes / Q000737:chemistry*; D006841:Hydrocarbons, Aromatic; D008956:Models, Chemical; D008958:Models, Molecular; D008968:Molecular Conformation; D015394:Molecular Structure; D011485:Protein Binding; D012984:Software
chemical_list: D001555:Benzene Derivatives; D002257:Carbonic Anhydrase Inhibitors; D005464:Fluorobenzenes; D006841:Hydrocarbons, Aromatic; D024402:Carbonic Anhydrase II