期刊
JOURNAL OF LUMINESCENCE
卷 132, 期 2, 页码 443-448出版社
ELSEVIER
DOI: 10.1016/j.jlumin.2011.09.027
关键词
Spectroscopy; Bovine serum albumin; Tosufloxacin tosylate; Interaction
类别
资金
- National Nature Science Foundation of China [20767004, 21177163]
- 111 Project [B08044]
- Fundamental Research Funds for the Central Universities [0910KYZY45]
- Minzu University of China (MUC) [98504-14, MUC 98507-08, MUC 02121103]
The interaction of tosufloxacin tosylate (TSFX) and bovine serum albumin (BSA) was studied by fluorescence spectroscopy, UV-vis spectroscopy and FT-IR spectroscopy. The results indicated that the intrinsic fluorescence of BSA was quenched by TSFX through a static quenching mechanism, and the effective binding constants (K-a,) were obtained by means of the modified Stern-Volmer equation. Thermodynamic parameters showed that electrostatic interaction was mostly responsible for the binding of TSFX to BSA. The binding distance (r) between TSFX and Trp-212 was determined to be 3.90 nm according to Foster non-radiative energy transfer theory. BSA had a single class of binding site at Sudlow' site I in subdomain IIA for TSFX. The effects of TSFX on the conformation of BSA were analyzed by synchronous fluorescence spectra and three-dimensional fluorescence spectra, and the results exhibited that the hydrophobicity of tryptophan microenvironment was decreased. In FT-IR spectra, Fourier self-deconvolution, secondary derivative and the curve-fitting process were carried out to obtain the components of BSA secondary structure at 298 K and 310 K. The full basic data indicated that the presence of TSFX resulted in alpha-helix and beta-sheet changing into beta-turn and random, which displayed that TSFX induced the unfolding of the polypeptides of BSA. (C) 2011 Elsevier B.V. All rights reserved.
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