Cell Biochemistry and Biophysics

, Volume 38, Issue 2, pp 215–237

Voltage-gated sodium channel toxins

Poisons, probes, and future promise

Authors

    • Department of Biochemistry, School of Medicine and Biomedical SciencesState University of New York
  • Anna L. Seibert
    • Department of Biochemistry, School of Medicine and Biomedical SciencesState University of New York
Review Article

DOI: 10.1385/CBB:38:2:215

Cite this article as:
Blumenthal, K.M. & Seibert, A.L. Cell Biochem Biophys (2003) 38: 215. doi:10.1385/CBB:38:2:215

Abstract

Neurotoxins have served as invaluable agents for identification, purification, and functional characterization of voltage-gated ion channels. Multiple classes of these toxins, which target voltage-gated Na+ channels via high-affinity binding to distinct but allosterically coupled sites, have been identified. The toxins are chemically diverse, including guanidinium heterocycles, a variety of structurally unrelated alkaloids, and multiple families of nonhomologous polypeptides having either related or distinct functions. This review describes the biochemistry and pharmacology of these agents, and summarizes the structure-function relationships underlying their interaction with molecular targets. In addition, we explore recent advances in the use of these toxins as molecular scaffolding agents, drugs, and insecticides.

Index Entries

Voltage-gated sodium channelpeptide neurotoxinsdrug designheart
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Copyright information

© Humana Press Inc 2003