Abstract
In this Letter we describe broad comparision studies toward rat, pig, and human aminopeptidase N (CD13) orthologs using phosphinate inhibitors related in structure to hydroxamic acids. This SAR approach yielded a very potent inhibitor of human aminopeptidase N: α 1-amino-3-phenylpropyl(α 2-hydroxy-3-phenylpropyl)phosphinic acid with an IC 50 = 60 nM.
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