Elsevier

Biochimie

Volume 92, Issue 11, November 2010, Pages 1509-1529
Biochimie

Review
Metallo-aminopeptidase inhibitors

https://doi.org/10.1016/j.biochi.2010.04.026Get rights and content

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.

Keywords

Aminopeptidase
Inhibitor
Non-covalent ligand
Drug design
Cancer
Malaria
Drugs
Diseases
Enzymes

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