title: Studies on binding interactions between clenbuterol hydrochloride and two serum albumins by multispectroscopic approaches in vitro.
abstract: In this study, binding properties of clenbuterol hydrochloride (CL) with human serum albumin (HSA) and bovine serum albumin (BSA) were examined using constant protein concentrations and various CL contents under physiological conditions. The binding parameters were confirmed using fluorescence quenching spectroscopy at various temperatures. The experimental results confirmed that the quenching mechanisms of CL and HSA/BSA were both static quenching processes. The thermodynamic parameters, namely, enthalpy change (ΔH) and entropy change (ΔS), were calculated according to the van't Hoff equation, which suggested that the electrostatic interactions were the predominant intermolecular forces in stabilizing the CL-HSA complex, and hydrogen bonds and van der Waals force were the predominant intermolecular forces in stabilizing the CL-BSA complex. Furthermore, the conformational changes of HSA/BSA in the presence of CL were determined using the data obtained from three-dimensional fluorescence spectroscopy, ultraviolet-visible absorption spectroscopy and circular dichroism spectroscopy.
authors.affiliation: School of Chemistry and Environment Science, Shaanxi University of Technology, Hanzhong Shaanxi, 723000, China.
authors.forename: Qin
authors.initials: Q
authors.lastname: Wang
authors.forename: Shengrui
authors.initials: S
authors.lastname: Zhang
mesh_terms: D000318:Adrenergic beta-Agonists / Q000737:chemistry*; D000818:Animals; D020240:Apraxia, Ideomotor; D001665:Binding Sites; D002417:Cattle; D002942:Circular Dichroism; D002976:Clenbuterol / Q000737:chemistry*; D006801:Humans; D006860:Hydrogen Bonding; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013816:Thermodynamics
chemical_list: D000318:Adrenergic beta-Agonists; D012709:Serum Albumin; D012710:Serum Albumin, Bovine; D002976:Clenbuterol
keywords: bovine serum albumin; clenbuterol hydrochloride; human serum albumin; interaction; spectroscopy