Abstract
A phosphinate analog of glutathionyl spermidine (Gsp), 3, has been synthesized and evaluated as an inhibitor of Gsp synthetase (GSPS). In addition, a non-spermidine-containing derivative ( 4) was synthesized in order to evaluate the role of the polyamine moiety in ligand binding. Compound 4 showed almost no inhibitory activity against E. coli GSPS while 3 was found to be a potent, slow-binding inhibitor of this enzyme, with the collisional E·I complex isomerizing to an E·I ∗ complex with 410-fold higher affinity.
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