کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1231046 | 1495200 | 2016 | 10 صفحه PDF | دانلود رایگان |
• Pin1 is governed by two types of quenching mechanisms.
• The higher concentration of EGCG could make the secondary structure of Pin1 change.
• Hydrogen bonds, electrostatic interaction and van der Waals interaction played the major role in the binding process.
• EGCG was bound to the Glu12, Lys13, Arg14, Met15 and Arg17 in WW domain,
• EGCG could interact with Arg69, Asp112, Cys113 and Ser114 in PPIase domain
The binding of epigallocatechin-3-gallate (EGCG) to wild type Pin1 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.
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Journal: Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy - Volume 169, 5 December 2016, Pages 134–143