Journal
JOURNAL OF FLUORESCENCE
Volume 20, Issue 2, Pages 507-516Publisher
SPRINGER/PLENUM PUBLISHERS
DOI: 10.1007/s10895-009-0574-8
Keywords
2,4-Dinitrophenol; 2,4-Dichlorphenol; Trypsin; Fluorescence spectroscopy; Binding constant
Funding
- Natural Science Foundation of Education Department of Jiangsu Province [07KJA18017]
- Educational Bureau [09KJD150007]
- Jiangsu Fundament
- Scientific Foundation of Yancheng Teachers University
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The interactions of 2, 4-dinitrophenol and 2, 4-dichlorphenol with trypsin were investigated by fluorescence, synchronous fluorescence, and three-dimensional fluorescence spectra techniques under physiological pH 7.40. The 2, 4-dinitrophenol and 2, 4-dichlorphenol effectively quenched the intrinsic fluorescence of trypsin via static quenching. The process of binding 2, 4-dinitrophenol and 2, 4-dichlorphenol with trypsin was a spontaneous molecular interaction procedure. The electrostatic repulsion does favor the interaction between 2, 4-DNP and trypsin. However, the interaction of 2, 4-DCP and trypsin can be explained on the basis of hydrogen bonding and van der Waals. The results of synchronous fluorescence spectroscopy and three-dimensional fluorescence spectra indicated that the structure of these trytophan and tyrosine residues environments were altered by 2, 4-DNP and 2, 4-DCP.
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