Validation of Antibody Toxin Fusions Against Sodium Channels

Poster Description

Achieving small molecule selectivity for ion channels can be challenging; therefore, peptide toxins have sparked considerable interest to advance both basic research and scaffold-based drug discovery. However, efficient isolation of the correctly folded peptide at a low cost is a current limitation. Recombinant expression of toxin peptides fused to a scaffold protein is an emerging strategy to overcome these production challenges, as well as enhancing in vivo stability of the toxin peptide.

Using automated patch clamp technology, we evaluate the potency and selectivity of ten NaV1.7-selective arachnid peptide toxins, which have been fused to the C-terminus (Fc region) of human IgG1.

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