Abstract
AbstractUnder 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 × 105 M−1 and 2.021 × 105 M−1, respectively. Thermodynamic parameter enthalpy change (ΔH) and entropy change (ΔS) were calculated to be ‐16.19 KJ/mol and 47.05 J·mol1·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.
Published Version
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