Steven A. Goldstein

A designer pore-blocking peptide reveals an electrostatic complementation mechanism for the inhibition-resistant Kv1.5 channel

Most voltage-gated potassium (Kv) channels are inhibited by peptide neurotoxins that occlude the pore with a positively-charged lysine. Kv1.5 repels these toxins electrostatically via four arginines (R487), one on each pore-forming subunit. Here, we describe chimera toxin (CmTx),...