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Identification of very potent inhibitor of human aminopeptidase N (CD13)

Authors
Journal
Bioorganic & Medicinal Chemistry Letters
0960-894X
Publisher
Elsevier
Publication Date
Volume
20
Issue
8
Identifiers
DOI: 10.1016/j.bmcl.2010.02.111
Keywords
  • Aminopeptidase N
  • Inhibitors
  • Hydroxamic Acid Analogues
  • Phosphinate

Abstract

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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