ArticleToxicon : official journal of the International Society on Toxinology2020
A centipede toxin causes rapid desensitization of nociceptor TRPV1 ion channel.
Article in Toxicon : official journal of the International Society on Toxinology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- From Discovery to the Future Medical Applications of Venom-derived Analgesic Peptides for the Treatment of Peripheral Pains.Current pharmaceutical design · 2026Review
- Neurotoxins Acting on TRPV1-Building a Molecular Template for the Study of Pain and Thermal Dysfunctions.Toxins · 2025Review
- Borneol's Pre-Clinical Analgesic Efficacy: Mediated by Receptor and Immune Mechanisms.Journal of pain research · 2025Review
- Design, synthesis and functional validation of peptide inhibitors based on TRPV1 ion channel agonist RhTx.Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2024Article
- Structure-guided peptide engineering of a positive allosteric modulator targeting the outer pore of TRPV1 for long-lasting analgesia.Nature communications · 2023Article
- Bioactive Peptides and Proteins from Centipede Venoms.Molecules (Basel, Switzerland) · 2022Review
- Centipede Venom: A Potential Source of Ion Channel Modulators.International journal of molecular sciences · 2022Review
- Venom Peptide Toxins Targeting the Outer Pore Region of Transient Receptor Potential Vanilloid 1 in Pain: Implications for Analgesic Drug Development.International journal of molecular sciences · 2022Review
- Rational Design of a Modality-Specific Inhibitor of TRPM8 Channel against Oxaliplatin-Induced Cold Allodynia.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Article
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.