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- W2008386617 abstract "Abstract Objective To provide a kinetic model(s) and reveal the mechanism of thymoquinone and Poloxin blocking an emerging anti-cancer target, human Polo-like kinase 1 (hPlk1) Polo-box domain (PBD). Methods The binding kinetics was determined by using a fluorescence polarization based assay. The putative mechanism was examined with a competition test. Results Thymoquinone follows a one-step binding with an association rate constant ( k 1 ) of 6.635×10 3 L·mol −1 ·min −1 . Poloxin fit a two-step binding with a dissociation constant (Ki) of 118 μmol/L for the intermediate complex and its isomerization rate ( k 4 ) of 0.131 5 min −1 to form an irreversible adduct. No significant dissociation was observed for either ligand up to 13 h. The inhibitors responded insignificantly to the presence of Michael donors as hPlk1-PBD competitors. Conclusion Thymoquinone and Poloxin are slow-tight ligands to the hPlk1-PBD with kinetic models distinct from each other. Michael addition as the mechanism is excluded." @default.
- W2008386617 created "2016-06-24" @default.
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- W2008386617 date "2010-06-01" @default.
- W2008386617 modified "2023-09-27" @default.
- W2008386617 title "Thymoquinone and Poloxin are slow-irreversible inhibitors to human Polo-like kinase 1 Polo-box domain" @default.
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- W2008386617 doi "https://doi.org/10.1016/s1000-1948(10)60032-9" @default.
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