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- W3044873550 abstract "Abstract In this research, we carried out spectral and computational methods to investigate the influence of galloyl moiety on Pin1. The fluorescence emission spectra revealed that the fluorescence quenching of Pin1 by epigallocatechin-3-gallate (EGCG) was a simultaneous dynamic and static quenching process, whereas the fluorescence quenching of Pin1 by epigallocatechin (EGC) was only a static quenching. In addition, the studies also indicated that the binding sites of EGCG and EGC to Pin1 were 2 and 1, respectively. Thermodynamic parameters, binding models, computational simulations and predicted binding free energy implied that hydrogen bonds, van der Waals and hydrophobic interactions were main binding forces in the Pin1-EGCG and Pin1-EGC systems. The synchronous and three-dimensional fluorescence, circular dichroism and Fourier transform infrared spectra illustrated that both EGCG and EGC could influence the conformation of Pin1. The fluorescence studies suggested that EGCG were bound to both the PPIase and WW domain, while EGC only was bound to the PPIase domain. The phenomena were further described using molecular docking and molecular dynamic simulations. Taken together, this research revealed that the inhibitory effect of EGCG on Pin1 was stronger than that of EGC, which was mainly due to the galloyl moiety." @default.
- W3044873550 created "2020-07-29" @default.
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- W3044873550 date "2020-10-01" @default.
- W3044873550 modified "2023-10-14" @default.
- W3044873550 title "Investigation on the influence of galloyl moiety to the peptidyl prolyl cis/trans isomerase Pin1: A spectral and computational analysis" @default.
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- W3044873550 doi "https://doi.org/10.1016/j.molliq.2020.113870" @default.
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