Interaction between varenicline tartrate and bovine serum albumin |
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| Authors: | Caifang Xun Yue Jiao Bingfei Jiang |
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| Institution: | 1. Key Laboratory of Theoretical Organic Chemistry and Functional Molecule, Ministry of Education, Hunan Province College Key Laboratory of QSAR/QSPR, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan, China;2. Nanjing Chemipioneer Pharma&3. Tech Co., Ltd, Nanjing, China |
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| Abstract: | This paper mainly investigated the interaction between varenicline tartrate and bovine serum albumin. The Stern–Volmer quenching constant and bimolecular quenching rate constant were determined; furthermore, the fluorescence quenching mechanism between varenicline tartrate and bovine serum albumin was clarified. The binding constants and the number of binding sites were deduced from the double logarithm regression curve. Thermodynamic parameters were calculated, which indicated that the binding process was spontaneous and the acting force were mainly hydrophobic forces. The binding distance was calculated to be 4.80 nm, which means that there was nonradiative energy transfer from varenicline tartrate to bovine serum albumin during the process. And the bovine serum albumin conformation affected by varenicline tartrate was analyzed through ultraviolet–visible and synchronous fluorescence spectroscopy. |
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| Keywords: | Bovine serum albumin fluorescence spectroscopy interaction ultraviolet-visible spectroscopy varenicline tartrate |
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