Abstract
The nociceptive transient receptor potential vanilloid 1 (TRPV1) ion channel is a polymodal receptor for multiple painful stimuli, hence actively pursued as a target for analgesic drugs. We identified a small peptide toxin RhTx2 from the Chinese red-headed centipede that strongly modulates TRPV1 activities. RhTx2, a 31-amino-acid peptide, is similar to a TRPV1-activating toxin RhTx we have previously discovered but with four extra amino acids at the N terminus. We observed that, like RhTx, RhTx2 activated TRPV1, but RhTx2 rapidly desensitized the channel upon prolonged exposure. Desensitization was achieved by reducing both the open probability and the single-channel conductance. RhTx2 is not only a tool to study the desensitization mechanism of TRPV1, but also a promising starting molecule for developing novel analgesics.
Original language | English (US) |
---|---|
Pages (from-to) | 41-49 |
Number of pages | 9 |
Journal | Toxicon |
Volume | 178 |
DOIs | |
State | Published - Apr 30 2020 |
Keywords
- Desensitization
- Gating mechanisms
- Nociception
- Peptide toxins
- TRPV1
ASJC Scopus subject areas
- Toxicology