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Biochimie. 2010 Nov;92(11):1509-29. doi: 10.1016/j.biochi.2010.04.026. Epub 2010 May 10.

Metallo-aminopeptidase inhibitors.

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1
Department of Bioorganic Chemistry, Faculty of Chemistry, Wrocław University of Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wrocław, Poland. artur.mucha@pwr.wroc.pl

Abstract

Aminopeptidases are enzymes that selectively hydrolyze an amino acid residue from the N-terminus of proteins and peptides. They are important for the proper functioning of prokaryotic and eukaryotic cells, but very often are central players in the devastating human diseases like cancer, malaria and diabetes. The largest aminopeptidase group include enzymes containing metal ion(s) in their active centers, which often determines the type of inhibitors that are the most suitable for them. Effective ligands mostly bind in a non-covalent mode by forming complexes with the metal ion(s). Here, we present several approaches for the design of inhibitors for metallo-aminopeptidases. The optimized structures should be considered as potential leads in the drug discovery process against endogenous and infectious diseases.

PMID:
20457213
DOI:
10.1016/j.biochi.2010.04.026
[Indexed for MEDLINE]
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