Journal
BIOCHIMIE
Volume 92, Issue 11, Pages 1509-1529Publisher
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.biochi.2010.04.026
Keywords
Aminopeptidase; Inhibitor; Non-covalent ligand; Drug design; Cancer; Malaria; Drugs; Diseases; Enzymes
Categories
Funding
- Foundation for Polish Science
- Polish Ministry of Science and Higher Education [N N302 159937]
- Canadian Institutes of Health Research (CIHR)
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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.
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