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Efficient Sialyltransferase Inhibitors Based on Transition-State Analogues of the Sialyl Donor
Bernd Müller1, Christoph Schaub1, Richard R Schmidt1
1Fakultät für Chemie der Universität, Fach M 725, D-78457 Konstanz (Germany), Fax: (+49) 7531-88-3135.
Abstract:
A 200- to 1000-fold higher affinity for sialyltransferase is shown by compounds 1 and 2 relative to the natural substrate. These inhibitors, which are derived from the transition state of SN 1-type sialyltransfer, contain a flat ring that is attached through a carbon atom with a phosphonate and a cytidine monophosphate group.
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