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

Renata Grzywa; Józef Oleksyszyn; Guy S Salvesen; Marcin Drag

doi:10.1016/j.bmcl.2010.02.111

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

Bioorg Med Chem Lett. 2010 Apr 15;20(8):2497-9. doi: 10.1016/j.bmcl.2010.02.111. Epub 2010 Mar 4.

Authors

Renata Grzywa¹, Józef Oleksyszyn, Guy S Salvesen, Marcin Drag

Affiliation

¹ Division of Medicinal Chemistry and Microbiology, Faculty of Chemistry, Wroclaw University of Technology, Wybrzeze Wyspianskiego, Wroclaw, Poland.

PMID: 20307982
DOI: 10.1016/j.bmcl.2010.02.111

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: alpha(1)-amino-3-phenylpropyl(alpha(2)-hydroxy-3-phenylpropyl)phosphinic acid with an IC(50)=60 nM.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
CD13 Antigens / antagonists & inhibitors*
Humans
Inhibitory Concentration 50
Protease Inhibitors / chemistry
Protease Inhibitors / pharmacology*

Substances

Protease Inhibitors
CD13 Antigens