Journal
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
Volume 169, Issue -, Pages 134-143Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2016.06.036
Keywords
Pin 1; Epigallocatechin-3-gallate; Fluorescence spectroscopy; Far-UV circular dichroism spectrum; Molecular dynamics simulations
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Funding
- National Key Technology R&D program of China [2006BAF07B01]
- Sichuan University
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The binding of epigallocatechin-3-gallate (EGCG) to wild type Pint in solution was studied by spectroscopic methods and molecular dynamics simulations in this research to explore the binding mode and inhibition mechanism. The binding constants and number of binding sites per Pin1 for EGCG were calculated through the Stern-Volmer equation. The values of binding free energy and thermodynamic parameters were calculated and indicated that hydrogen bonds, electrostatic interaction and Van der Waals interaction played the major role in the binding process. The alterations of Pin1 secondary structure in the presence of EGCG were confirmed by far-UV circular dichroism spectra. The binding model at atomic-level revealed that EGCG was bound to the Glu12, Lys13, Arg14, Met15 and Arg17 in WW domain. Furthermore, EGCG could also interact with Arg69, Asp112, Cys113 and Ser114 in PPIase domain. (C) 2016 Elsevier B.V. All rights reserved.
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