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Updated: May 18, 2026
Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)
Published on: August 31, 2018
A study on the interaction between 3-spiro-piperidones and bovine serum albumin using spectroscopic approaches
Xianyong Yu1, Qing Yao, Hongwen Tao
1Key Laboratory of Theoretical Chemistry and Molecular Simulation of Ministry of Education, Hunan Province College Key Laboratory of QSAR/QSPR, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan, 411201, People's Republic of China.
Abstract:
The interaction between 3-spiro-2'-pyrrolidine-3'-spiro-3″-piperidine-2,3″-dione (PPD) and bovine serum albumin (BSA) in aqueous solution was studied using fluorescence and UV-vis spectroscopy. Fluorescence emission data revealed that BSA (1.00 × 10(-5) mol/L) fluorescence was statically quenched by PPD at various concentrations, which implies that a PPD-BSA complex was formed. The binding constant (KA ), the number of binding sites (n) and the specific binding site of the PPD with BSA were determined. Energy-transfer efficiency parameters were determined and the mechanism of the interaction discussed. The thermodynamic parameters, ΔG, ΔH and ΔS, were obtained according to van't Hoff's equation, showing the involvement of hydrophobic forces in these interactions. The effect of PPD acting on the BSA conformation was detected by synchronous fluorescence.
