Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5403161 | Journal of Luminescence | 2007 | 7 Pages |
Abstract
The binding of 3-(p-bromophenyl)-5-methyl-thiohydantoin (BPMT) with human serum albumin (HSA) was investigated by fluorescence spectroscopy in combination with UV absorption spectrum under physiological conditions. The intrinsic fluorescence of HSA was quenched by BPMT through static quenching mechanism and the fluorescence emission spectrum of HSA exhibited appreciable hypsochromic shift with increasing concentration of BPMT. The binding constants (K) of HSA with BPMT and the number binding sites (n) at different temperatures, thermodynamic parameter enthalpy changes (ÎH) and entropy changes (ÎS) of HSA-BPMT have been calculated according to the relevant fluorescence data, indicating that the hydrophobic interaction played a major role, which was consistent with the result of molecular modeling study.
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Authors
Fengling Cui, Junli Wang, Yanrui Cui, Jianping Li, Xiaojun Yao, Yan Lu, Jing Fan,