A study on the interaction between 3‐spiro‐piperidones and bovine serum albumin using spectroscopic approaches. (4th September 2012)

• Record Type: Journal Article
• Authors: Yu, Xianyong; Yao, Qing; Tao, Hongwen; Yang, Ying; Li, Lei; Zheng, Baishu; Zhu, Shizhong
• Is Part Of: Luminescence. Volume 28:Number 5(2013:Sep./Oct.)
• Page Start: 705
• Page End: 712
• Publication Date: 2012-09-04
• Subjects: Luminescence -- Periodicals; Bioluminescence -- Periodicals; Chemiluminescence -- Periodicals; Luminescence -- Periodicals; 535.35
• DOI: 10.1002/bio.2420
• Languages: English
• ISSNs: 1522-7235

Abstract

<abstract abstract-type="main"> <title>ABSTRACT</title> <p>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 (<italic>K_A</italic>), the number of binding sites (<italic>n</italic>) 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<italic>G</italic>, Δ<italic>H</italic> and Δ<italic>S</italic>, 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 &amp; Sons, Ltd.</p> </abstract>