Identification and characterization of small molecule modulators of KChIP/Kv4 function

Inhibitors have been identified which modulate the Kv4/KChIP potassium channel complex. The apparent affinity of KChIP1 to Kv4.3-N and the current amplitude and kinetics were altered with compound exposure. Fluorescence spectroscopy and molecular modeling of the KChIP1 crystal structure indicate that compound binding may occur in a small tryptophan-containing pocket on the hydrophilic side of the protein.