Fluorescent investigation of the interactions between N-(p-chlorophenyl)-N'-(1-naphthyl) thiourea and serum albumin:: Synchronous fluorescence determination of serum albumin

被引：113

作者：

Cui, Feng-Ling ^{[1
]}

Wang, Jun-Li ^{[1
]}

Cui, Yan-Rul ^{[1
]}

Li, J'an-Ping ^{[1
]}

机构：

[1] Henan Normal Univ, Key Lab Environm Pollut Control Technol Henan Pro, Sch Chem & Environm Sci, Xinxiang 453007, Hennan, Peoples R China

来源：

ANALYTICA CHIMICA ACTA | 2006年 / 571卷 / 02期

关键词：

N-(p-chlorophenyl)-N'-(1-naphthyl) thiourea (CPNT); bovine serum albumin (BSA); human serum albumin (HSA); flourescence spectroscopy; synchronous flourescence;

D O I：

10.1016/j.aca.2006.05.002

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

The interactions between N-(p-chlorophenyl)-N'-(1-napthyl) thiourea and serum albumin were investigated by fluorescence spectroscopy and UV absorption spectrum under physiological conditions. The results of spectroscopic measurements suggested that N-(p-chlorophenyl)-N'-(1-naphthyl) thiourea should have a strong ability to quench the intrinsic fluorescence of both bovine serum albumin and human serum albumin through static quenching procedure. and the hydrophobic interaction was the predominant intermolecular force stabilizing the complex. Thermodynamic parameter enthalpy changes (Delta H) and entropy changes (Delta S) were calculated according to the Vant' Hoff equation. The binding distances between N-(p-chlorophenyl)-N'-(1-naphthyl) thiourea and the proteins were evaluated on the basis of the theory of Foster energy transfer. In addition, the effects of other ions on the binding constants of complexes were also discussed. Synchronous fluorescence technology was successfully applied to the determination of serum albumins added to the CPNT Solution. (c) 2006 Elsevier B.V. All rights reserved.

引用

页码：175 / 183

页数：9

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