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|Title:||Synthesis and biological evaluation of guanidino compounds endowed with subnanomolar affinity as competitive inhibitors of maize polyamine oxidase||Authors:||Manetti, Fabrizio
ZIZZARI A., T
|Issue Date:||2009||Project:||None||Journal:||JOURNAL OF MEDICINAL CHEMISTRY||Abstract:||
Previous studies on agmatine and its derivatives suggested that the presence of hydrophobic groups on the guanidine moiety was a crucial key for inhibitory activity of maize polyamine oxidase. Accordingly, new lipophilic agmatine and iminoctadine derivatives were synthesized and tested for their ability to inhibit this enzyme. Several compounds showed an affinity in the nanomolar range, while a cyclopropylmethyl derivative of iminoctadine was found to be the most potent inhibitor of maize polyamine oxidase reported so far (Ki = 0.08 nM).
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