title: Electrochemical studies of the interaction of clarithromycin with bovine serum albumin.
abstract: The interaction of clarithromycin (CAM) with bovine serum albumin (BSA) was investigated in pH 4.5-8.0 phosphate buffer solutions in which three irreversible reduction waves P(1), P(2) and P(3) of CAM appeared on linear-sweep voltammetry on a static dropping mercury working electrode. In the acidic media, with the addition of BSA into the CAM solution, a new electrochemically active complex was formed and there was interaction between the carbonyl group C=O in the C-9 position of CAM and BSA. It was found that electrostatic and hydrophobic forces played an important role in the binding reaction. However, new electrochemically non-active complexes were formed at physiological pH condition. The study showed that the formation constant and formation ratio of the interaction between CAM and BSA were 1.51 x 10(12) and 3:1 for P(2) wave, and 4.53 x 10(5) and 1:1 for P(3) wave, respectively. The ion strength enhanced the hydrophobic interaction between CAM and BSA.
authors.affiliation: College of Sciences, Xi'an University of Architecture and Technology, Shaanxi 710055, PR China. dshiney2004@yahoo.com.cn
authors.forename: She-Ying
authors.initials: SY
authors.lastname: Dong
authors.forename: Chun-Xia
authors.initials: CX
authors.lastname: Xue
authors.forename: Ting-Lin
authors.initials: TL
authors.lastname: Huang
mesh_terms: D000143:Acids / Q000737:chemistry; D000818:Animals; D002021:Buffers; D020134:Catalytic Domain; D002417:Cattle; D017291:Clarithromycin / Q000737:chemistry* / Q000378:metabolism; D004563:Electrochemistry; D006863:Hydrogen-Ion Concentration; D009994:Osmolar Concentration; D010084:Oxidation-Reduction; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism
chemical_list: D000143:Acids; D002021:Buffers; D012710:Serum Albumin, Bovine; D017291:Clarithromycin