Voltage-gated sodium channel toxins: Poisons, probes, and future promise

Authors: Blumenthal, Kenneth¹; Seibert, Anna²

Source: Cell Biochemistry and Biophysics, Volume 38, Number 2, June 2003 , pp. 215-237(23)

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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.

Keywords: Voltage-gated sodium channel; peptide neurotoxins; drug design; heart

Document Type: Research article

DOI: http://dx.doi.org/10.1385/CBB:38:2:215

Affiliations: 1: Department of Biochemistry, School of Medicine and Biomedical Sciences, State University of New York, 14214, Buffalo, NY, Email: kblumen@buffalo.edu 2: Department of Biochemistry, School of Medicine and Biomedical Sciences, State University of New York, 14214, Buffalo, NY,

Publication date: 2003-06-01