Metallo-aminopeptidase inhibitors

A. Mucha, M. Drag, John Dalton, P. Kafarski

Research output: Contribution to journalArticlepeer-review

85 Citations (Scopus)

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. Crown Copyright (C) 2010 Published by Elsevier Masson SAS. All rights reserved.
Original languageEnglish
Pages (from-to)1509-1529
Number of pages21
JournalBiochimie
Volume92
Issue number11
DOIs
Publication statusPublished - Nov 2010

ASJC Scopus subject areas

  • Biochemistry

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