Journal
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
Volume 116, Issue -, Pages 251-257Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2013.07.035
Keywords
Cinnamic acid; Trypsin; Inhibition; Binding mode; Molecular modeling
Categories
Funding
- Fund for the National Natural Science Foundation of China [21201147]
- Natural Science Foundation of Jiangsu Province [BK2011422, BK2012671]
- Natural Science Foundation of Education Department of Jiangsu Province [11KJB150019]
- Jiangsu Fundament of Qilan Project
- Jiangsu Fundament of 333 Project
- Scientific Foundation of Yancheng Teachers University
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In order to investigate the association of the protease trypsin with cinnamic acid, the interaction was characterized by using fluorescence, UV-vis absorption spectroscopy, molecular modeling and an enzymatic inhibition assay. The binding process may be outlined as follows: cinnamic acid can interact with trypsin with one binding site to form cinnamic acid-trypsin complex, resulting in inhibition of trypsin activity; the spectroscopic data show that the interaction is a spontaneous process with the estimated enthalpy and entropy changes being -8.95 kJ mol(-1) and 50.70 J mol(-1) K-1, respectively. Noncovalent interactions make the main contribution to stabilize the trypsin-cinnamic acid complex; cinnamic acid can enter into the primary substrate-binding pocket and alter the environment around Trp and Tyr residues. (C) 2013 Elsevier B.V. All rights reserved.
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