Binding study of sulfonylureas and phenothiazines to bovine serum albumin using difference spectrophotometry.
2-(4'-Hydroxybenzeneazo)benzoic acid is a spectrophotometric probe which shows absorption spectrum changes upon binding to protein. Difference absorption spectra of this probe were used as an indirect measurement of the binding of selected sulfonylurea and phenothiazine drugs to bovine serum albumin. The results obtained using the spectrophotometric probe were similar to data obtained from other methods, especially fluorescent methods. Of the four sulfonylureas studied, tolbutamide showed the highest binding affinity, followed by glyburide, glipizide, and acetohexamide, in that order. The data collected for phenothiazine drugs indicated that chlorpromazine has the highest affinity, followed in order by trifluoperazine, perphenazine, fluphenazine, and promazine. Correlation of these results with chemical composition indicated that the interaction of phenothiazine drugs with bovine serum albumin was of a hydrophobic nature.
D000818:Animals; D001667:Binding, Competitive; D002417:Cattle; D010640:Phenothiazines / Q000378:metabolism*; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D012995:Solubility; D013056:Spectrophotometry, Ultraviolet; D013453:Sulfonylurea Compounds / Q000378:metabolism*
D010640:Phenothiazines; D013453:Sulfonylurea Compounds; D012710:Serum Albumin, Bovine