期刊
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
卷 83, 期 1, 页码 130-135出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2011.07.092
关键词
Trypsin; Sodium benzoate; Toxicity; Spectroscopy; Molecule docking
类别
资金
- Natural Science Foundation of China [20875055]
- Ministry of Education of China [708058]
- Key Science-Technology Project in Shandong Province [2008GG10006012]
The toxicity of sodium benzoate to trypsin was investigated by fluorescence spectroscopy, synchronous fluorescence spectroscopy, UV-visible absorption spectroscopy and circular dichroism (CD) spectroscopy under mimic physiological conditions. Sodium benzoate could unfold trypsin by decreasing the beta-sheet structure, which leads to more exposure of internal amino acid groups and the obvious intrinsic fluorescence quenching with the rising concentration of sodium benzoate. The results of spectroscopic measurements indicated that sodium benzoate changed the internal microenvironment of trypsin and induced the alteration of the whole molecule, which were performed toxic effects on the organism. Trypsin and sodium benzoate interacted with each other to produce a substance by van der Waals forces and hydrogen bond, the model of which was shown by AutoDock software. (C) 2011 Elsevier B.V. All rights reserved.
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