期刊
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
卷 105, 期 -, 页码 74-79出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2012.11.064
关键词
Chloroamphenicol; Bovine serum albumin; Fluorescence spectroscopy; UV-visible spectroscopy; Metal ions; Displacement experiments
类别
资金
- National Natural Science Foundation of China [51103122]
- Natural Science Foundation of the Fujian Province for the Youth [2011J05137]
- Scientific Research Foundation of Fuzhou University [022386]
The binding of chloroamphenicol (CPC) to bovine serum albumin (BSA) at 296 K, 303 K, and 310 K by fluorescence and UV-visible absorption spectroscopy were investigated under imitated physiological conditions. The experimental results showed that the fluorescence quenching mechanism between CPC and BSA was combined quenching (dynamic and static quenching) procedure at low CPC concentration, or a dynamic quenching procedure at high concentrations. The binding constants, binding sites and the corresponding thermodynamic parameters of the interaction system were calculated. According to Forster non-radiation energy transfer theory, the binding distance between CPC and BSA was calculated to be 3.02 nm. Both synchronous fluorescence and FT-IR spectra confirmed the interaction, and indicated the conformational changes of BSA. The effects of some common metal ions Ca2+, Ni2+, Mg2+, Fe2+, and Cu2+ on the binding constant between CPC and BSA were examined. Furthermore, we investigated the possible sub-domains on BSA that bind CPC by displacement experiments. (C) 2012 Published by Elsevier B.V.
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