Insights into the binding mode and functional components of the analgesic-antitumour peptide from Karsch to human voltage-gated sodium channel 1.7 based on dynamic simulation analysis.

Voltage-gated sodium (Na) channels are transmembrane proteins composed of four homologous domains (DI-DIV) that play important roles in membrane excitability in neurons and muscles. Analgesic-antitumour peptide (AGAP) is a neurotoxin from the scorpion Karsch, and has been shown to exert analgesic effect by binding on site 4 of human Na1.7 (hNa1.