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Investigation of the Interaction between N,N′‐Di(4‐Chlorophenyl)Thiourea and Human Serum Albumin by Fluorescence Spectroscopy: Synchronous Fluorescence Determination of Human Serum Albumin
Author(s) -
Cui FengLing,
Wang JunLi,
Cui YanRui,
Li JianPing
Publication year - 2007
Publication title -
journal of the chinese chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.329
H-Index - 45
eISSN - 2192-6549
pISSN - 0009-4536
DOI - 10.1002/jccs.200700075
Subject(s) - chemistry , thiourea , human serum albumin , fluorescence , quenching (fluorescence) , fluorescence spectroscopy , enthalpy , analytical chemistry (journal) , serum albumin , absorption (acoustics) , chromatography , organic chemistry , biochemistry , thermodynamics , physics , quantum mechanics , acoustics
Under physiological conditions, interaction between N,N′‐di(4‐chlorophenyl)thiourea synthesized and human serum albumin was investigated by using fluorescence spectroscopy and UV absorption spectrum. The intrinsic fluorescence of human serum albumin was quenched by N,N′‐di(4‐chlorophenyl)‐thiourea through a static quenching procedure. The binding constants (K) at 14 °C and 24 °C were obtained, and the values were 2.541 × 10 5 M −1 and 2.021 × 10 5 M −1 , respectively. Thermodynamic parameter enthalpy change (ΔH) and entropy change (ΔS) were calculated to be ‐16.19 KJ/mol and 47.05 J·mol 1 ·K −1 , respectively, which indicated that hydrophobic force played a major role in interaction. The binding distance was evaluated on the basis of the theory of Föster energy transfer. The effects of various metal ions on the binding constants of N,N′‐di(4‐chlorophenyl)thiourea with human serum albumin were studied. A synchronous fluorescence technique for determination of human serum albumin was developed, and the method was successfully applied to the detection of HSA in human serum samples.