ArticleThe Journal of biological chemistry2016
Interaction of Tarantula Venom Peptide ProTx-II with Lipid Membranes Is a Prerequisite for Its Inhibition of Human Voltage-gated Sodium Channel NaV1.7.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 69 citations in OpenAlex.
- Review
- Structural basis of inhibition of human NaNature communications · 2025Article
- δ-Conotoxin Structure Prediction and Analysis through Large-Scale Comparative and Deep Learning Modeling Approaches.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Structural basis of inhibition of human NabioRxiv : the preprint server for biology · 2024Article
- Elucidating molecular mechanisms of protoxin-II state-specific binding to the human NaV1.7 channel.The Journal of general physiology · 2024Article
- Structure-function and rational design of a spider toxin Ssp1a at human voltage-gated sodium channel subtypes.Frontiers in pharmacology · 2023Article
- The Tarantula Toxin ω-Avsp1a Specifically Inhibits Human CaBiomedicines · 2022Article
- Pharmacological Inhibition of the Voltage-Gated Sodium Channel NaACS pharmacology & translational science · 2021Article
- Potency-Enhancing Mutations of Gating Modifier Toxins for the Voltage-Gated Sodium Channel NaToxins · 2021Article
- Pain-related toxins in scorpion and spider venoms: a face to face with ion channels.The journal of venomous animals and toxins including tropical diseases · 2021Review
- Engineering of a Spider PeptideFrontiers in molecular biosciences · 2021Article
- Voltage-Gated Sodium Channel Modulation by a New Spider Toxin Ssp1a Isolated From an Australian Theraphosid.Frontiers in pharmacology · 2021Article
- Sample preparation of the human TRPA1 ion channel for cryo-EM studies.Methods in enzymology · 2021Article
- Cyclic peptide scaffold with ability to stabilize and deliver a helical cell-impermeable cargo across membranes of cultured cancer cells.RSC chemical biology · 2020Article
- Article
- Characterisation of d-Conotoxin TxVIA as a Mammalian T-Type Calcium Channel Modulator.Marine drugs · 2020Article
- Employing NaChBac for cryo-EM analysis of toxin action on voltage-gated NaProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Mapping the Molecular Surface of the Analgesic NaACS pharmacology & translational science · 2020Article
- Manipulation of a spider peptide toxin alters its affinity for lipid bilayers and potency and selectivity for voltage-gated sodium channel subtype 1.7.The Journal of biological chemistry · 2020Article
- A Chemical Biology Approach to Probing the Folding Pathways of the Inhibitory Cystine Knot (ICK) Peptide ProTx-II.Frontiers in chemistry · 2020Article
Corrections and comments
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Authors and funding
12 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ProTx-II is a disulfide-rich peptide toxin from tarantula venom able to inhibit the human voltage-gated sodium channel 1.7 (hNaV1.7), a channel reported to be involved in nociception, and thus it might have potential as a pain therapeutic. ProTx-II acts by binding to the membrane-embedded voltage sensor domain of hNaV1.7, but the precise peptide channel-binding site and the importance of membrane binding on the inhibitory activity of ProTx-II remain unknown. In this study, we examined the structure and membrane-binding properties of ProTx-II and several analogues using NMR spectroscopy, surface plasmon resonance, fluorescence spectroscopy, and molecular dynamics simulations. Our results show a direct correlation between ProTx-II membrane binding affinity and its potency as an hNaV1.7 channel inhibitor. The data support a model whereby a hydrophobic patch on the ProTx-II surface anchors the molecule at the cell surface in a position that optimizes interaction of the peptide with the binding site on the voltage sensor domain. This is the first study to demonstrate that binding of ProTx-II to the lipid membrane is directly linked to its potency as an hNaV1.7 channel inhibitor.
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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.