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- W3082989080 endingPage "112776" @default.
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- W3082989080 abstract "A set of fluorinated sialyl-T derivatives were efficiently synthesized using one-pot multi-enzyme (OPME) chemoenzymatic approach. The P. multocida α2–3-sialyltransferase (PmST1) involved in the synthesis showed extremely flexible donor and acceptor substrate specificities. These sialosides have been successfully investigated with stability towards Clostridium perfringens sialidase substrate specificity assay using 1H NMR spectroscopy. Hydrolysis studies monitored by 1H NMR clearly demonstrated that the fluorine substitution obviously reduced hydrolysis rate of Clostridium perfringens sialidase. To further investigate the fluorine influence, structure-dependent variation of sialoside-lectin binding was observed for MAL and different sialoside-immobilized surfaces. Subtle changes on the ligand of carbohydrate-binding protein were distinguished by SPR. These fluorinated sialyl-T derivatives obtained are valuable probes for further biological studies or antitumor drug design." @default.
- W3082989080 created "2020-09-08" @default.
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- W3082989080 date "2020-12-01" @default.
- W3082989080 modified "2023-09-25" @default.
- W3082989080 title "Efficient chemoenzymatic synthesis of fluorinated sialyl Thomsen–Friedenreich antigens and investigation of their characteristics" @default.
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- W3082989080 doi "https://doi.org/10.1016/j.ejmech.2020.112776" @default.
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