The zinc finger proteins have fascinated many research groups because of their modular assembly, broad range of biological functions and more recently because they are attractive targets for antiviral therapy. The zinc finger domain is a very stable structural element whose hallmark is the coordination of a zinc ion by several amino acid residues, usually cysteines and histidines. These structural motifs are associated with protein-nucleic acid recognition as well as protein-protein interactions. The biological function of the zinc finger proteins is strongly dependent on the zinc ion, which assure integrity and stability. Thus, the disruption of critical zinc finger viral proteins represents a fundamentally new approach to inhibit viral replication in the absence of mutations leading to drug resistance phenotypes. This review summarizes the drug design and potential therapeutic applications of viral zinc fingers disrupting agents for the control of viral diseases.
Keywords: Structural domains, zinc fingers, antiviral, oxidizing compounds, human immunodeficiency virus, arenavirus
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