Studies on the interactions of 2, 4-dinitrophenol and 2, 4-dichlorphenol with trypsin.

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.