Engineering of highly potent and selective HNTX-III mutant against hNa1.7 sodium channel for treatment of pain.

Human voltage-gated sodium channel Na1.7 (hNa1.7) is involved in the generation and conduction of neuropathic and nociceptive pain signals.

Scorpion toxin inhibits the voltage-gated proton channel using a Zn -like long-range conformational coupling mechanism.

Background And Purpose: Blocking the voltage-gated proton channel H 1 is a promising strategy for the treatment of diseases like ischaemia stroke and cancer. However, few H 1 channel antagonists have been reported. Here, we have identified a novel H 1 channel antagonist from scorpion venom and have elucidated its action mechanism.

Discovery of a Novel Na1.7 Inhibitor From Venom With Potent Analgesic Efficacy.

Spider venoms contain a vast array of bioactive peptides targeting ion channels. A large number of peptides have high potency and selectivity toward sodium channels. Na1.

µ-TRTX-Ca1a: a novel neurotoxin from Cyriopagopus albostriatus with analgesic effects.

Human genetic and pharmacological studies have demonstrated that voltage-gated sodium channels (VGSCs) are promising therapeutic targets for the treatment of pain. Spider venom contains many toxins that modulate the activity of VGSCs. To date, only 0.

Engineering Gain-of-Function Analogues of the Spider Venom Peptide HNTX-I, A Potent Blocker of the hNa1.7 Sodium Channel.

Pain is a medical condition that interferes with normal human life and work and reduces human well-being worldwide. The voltage-gated sodium channel (VGSC) human Na1.7 (hNa1.