Abstract
Spider venoms contain an evolutionarily honed pharmacopeia of natural toxins that target membrane receptors and ion channels to produce shock, paralysis, pain, or death. Toxins evolve to interact with functionally important protein domains, including agonist binding sites, ion permeation pores, and voltage-sensing domains, making them invaluable reagents with which to probe mechanisms underlying channel activation or modulation. We have identified a novel tarantula peptide toxin that serves as an irreversible agonist for the heat/capsaicin-activated channel, TRPV1. The toxin contains two independently functional Inhibitor Cysteine Knot (ICK) domains, endowing it with an antibody-like bivalency that results in extremely high avidity for its multimeric channel target. We are using this new toxin as a tool to help dissect the unique properties of TRPV1.
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