ProTx-II, an effective and selective NaV1.7 channel blocker, shifts activation gating positively and decreases current magnitude. It blocks action potential propagation in nociceptors.
CAT No: R0894
CAS No:484598-36-9
Synonyms/Alias:ProTx II;484598-36-9;ProTx-II;PTX-3995-PI;JUA59836;AKOS024457935;PD079626;
ProTx II is a peptide neurotoxin originally isolated from the venom of the tarantula Thrixopelma pruriens, recognized for its potent and selective modulation of voltage-gated sodium channels, particularly Nav1.7. As a member of the cystine knot peptide family, ProTx II exhibits a compact and stable structure, enabling high-affinity interactions with its molecular targets. Its specificity and functional activity have made it a valuable molecular probe in neurophysiological research, ion channel pharmacology, and the broader study of pain signaling pathways. The compound's unique mode of action and well-defined biochemical profile support its widespread adoption in both academic and industrial research settings focused on ion channel function and modulation.
Electrophysiological Research: ProTx II is extensively utilized as a selective inhibitor of the Nav1.7 voltage-gated sodium channel in electrophysiological studies. Researchers employ this peptide to dissect the functional roles of Nav1.7 and related channels in neuronal excitability, action potential propagation, and synaptic transmission. By applying ProTx II in patch-clamp or voltage-clamp experiments, scientists are able to precisely characterize channel kinetics, gating mechanisms, and pharmacological sensitivities, facilitating a deeper understanding of neuronal signaling and ion channelopathies.
Ion Channel Drug Discovery: The peptide's high selectivity for Nav1.7 has positioned it as a critical tool compound in the early stages of ion channel-targeted drug discovery. Pharmaceutical and biotechnology laboratories use ProTx II to validate Nav1.7 as a therapeutic target, screen for small molecule modulators, and benchmark the efficacy and selectivity of new channel inhibitors. Its application in assay development and high-throughput screening platforms accelerates the identification and optimization of candidate molecules for further preclinical research.
Pain Pathway Elucidation: Due to its ability to block Nav1.7-mediated sodium currents, ProTx II serves as a molecular probe for investigating the role of this channel in pain perception and nociceptive signaling. Experimental models incorporating the peptide allow researchers to delineate the contribution of Nav1.7 to sensory neuron function, spinal cord processing, and peripheral pain pathways. These studies provide critical mechanistic insights into the molecular underpinnings of pain and support the development of novel strategies for pain research.
Peptide Structure-Function Studies: The well-characterized cystine knot motif and defined pharmacophore of ProTx II make it an ideal subject for studies examining peptide structure-activity relationships. Through site-directed mutagenesis, chemical modification, or biophysical analysis, scientists can probe the specific residues and structural features responsible for channel binding and modulation. Such research advances the fundamental understanding of peptide-channel interactions and informs the rational design of next-generation peptide modulators.
Toxin Engineering and Synthetic Biology: ProTx II's robust stability and defined activity profile render it a valuable template for toxin engineering and synthetic biology applications. By leveraging its structure, researchers can design and synthesize analogs with altered specificity, potency, or biophysical properties for use in custom research tools or biosensors. These engineered variants expand the toolkit available for probing ion channel function and enable the creation of novel peptide-based reagents tailored to specific experimental requirements.
The tarantula venom peptides ProTx-I and ProTx-II inhibit voltage-gated sodium channels by shifting their voltage dependence of activation to a more positive potential, thus acting by a mechanism similar to that of potassium channel gating modifiers such as hanatoxin and VSTX1. ProTx-I and ProTx-II inhibit all sodium channel (Nav1) subtypes tested with similar potency and represent the first potent peptidyl inhibitors of TTX-resistant sodium channels. Like gating modifiers of potassium channels, ProTx-I and ProTx-II conform to the inhibitory cystine knot motif, and ProTx-II was demonstrated to bind to sodium channels in the closed state.
ProTx-I and ProTx-II: Gating modifiers of voltage-gated sodium channels
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