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A study on the interaction between 3‐spiro‐piperidones and bovine serum albumin using spectroscopic approaches
Author(s) -
Yu Xianyong,
Yao Qing,
Tao Hongwen,
Yang Ying,
Li Lei,
Zheng Baishu,
Zhu Shizhong
Publication year - 2012
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.2420
Subject(s) - bovine serum albumin , chemistry , fluorescence , piperidine , pyrrolidine , aqueous solution , fluorescence spectroscopy , hydrophobic effect , binding constant , förster resonance energy transfer , binding site , serum albumin , chromatography , analytical chemistry (journal) , stereochemistry , organic chemistry , biochemistry , physics , quantum mechanics
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 ( K A ), 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, Δ G , Δ H and Δ S , 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. Copyright © 2012 John Wiley & Sons, Ltd.