Journal
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
Volume 118, Issue -, Pages 510-519Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2013.09.027
Keywords
Trypsin; Bicyclol; Analogs; Interaction
Categories
Funding
- National Natural Science Foundation of China [21172202, 20905065]
- Key science and technology plan project of Henan province [132102110051]
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The interactions between Trypsin and Bicyclol or analogs (Bifendate, I, II and III) were investigated by spectrophotometric methods. It was found that Bicyclol or analogs had strong ability to quench the intrinsic fluorescence of Trypsin by a static quenching procedure. The binding constants were obtained at three temperatures. The thermodynamics parameters reveal that the hydrophobic and electrostatic interactions play an important role in the interaction. Results showed that the microenvironments of tryptophan residue of Trypsin were disturbed by the analogs. Results indicated that Bifendate was the strongest quencher among five compounds. (C) 2013 Elsevier B.V. All rights reserved.
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