Studies on binding interactions between clenbuterol hydrochloride and two serum albumins by multispectroscopic approaches in vitro

作者：Wang Qin^*; Zhang Shengrui

来源：Luminescence, 2014, 29(5): 492-499.

DOI：10.1002/bio.2574

• clenbuterol hydrochloride
• human serum albumin
• bovine serum albumin
• interaction
• spectroscopy

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 (Delta H) and entropy change (Delta S), 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.

• 出版日期2014-8
• 单位陕西理工大学