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Related Concept Videos

Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

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Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several...
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Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

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Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
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Resting Membrane Potential01:24

Resting Membrane Potential

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The relative difference in electrical charge, or voltage, between the inside and the outside of a cell membrane, is called the membrane potential. It is generated by differences in permeability of the membrane to various ions and the concentrations of these ions across the membrane.
The Inside of a Neuron is More Negative
The membrane potential of a cell can be measured by inserting a microelectrode into a cell and comparing the charge to a reference electrode in the extracellular fluid. The...
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Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

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Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that...
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The Resting Membrane Potential01:21

The Resting Membrane Potential

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Overview
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Nondepolarizing (Competitive) Neuromuscular Blockers: Mechanism of Action01:17

Nondepolarizing (Competitive) Neuromuscular Blockers: Mechanism of Action

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Nondepolarizing neuromuscular blockers induce paralysis by competitively blocking nicotinic acetylcholine receptors at the muscle end plate. Examples include pancuronium, mivacurium, vecuronium, and rocuronium. These quaternary ammonium derivatives are administered intravenously, are poorly absorbed, and are excreted via the kidneys.
Competitive antagonists prevent acetylcholine from binding to its receptor, inhibiting membrane depolarization. Without conformational changes or intrinsic...
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Related Experiment Video

Updated: Jul 5, 2025

Vibrodissociation of Neurons from Rodent Brain Slices to Study Synaptic Transmission and Image Presynaptic Terminals
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Voltage-Gated Sodium Channel Inhibition by µ-Conotoxins.

Kirsten L McMahon1, Irina Vetter1,2, Christina I Schroeder1,3

  • 1Institute for Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia.

Toxins
|January 22, 2024
PubMed
Summary
This summary is machine-generated.

µ-Conotoxins are potent blockers of sodium channels, but their subtype promiscuity limits therapeutic use. This review details conotoxin interactions, structure-activity relationships, species selectivity, and disulfide connectivity to guide analgesic development.

Keywords:
disulfide-rich peptidepeptidestructure–activity relationshipssubtype selectivityvenom peptidevoltage-gated sodium channelsµ-conotoxin

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Area of Science:

  • Pharmacology
  • Neuroscience
  • Biochemistry

Background:

  • µ-Conotoxins are potent inhibitors of voltage-gated sodium (NaV) channels.
  • They serve as valuable pharmacological tools and potential candidates for pain relief.
  • Subtype promiscuity of µ-conotoxins leads to undesired side effects, hindering therapeutic application.

Purpose of the Study:

  • To review current research on µ-conotoxins.
  • To elucidate interactions between µ-conotoxins and various NaV channel subtypes.
  • To explore structure-activity relationships, species selectivity, and disulfide connectivity impacts on conotoxin activity.

Main Methods:

  • Review of existing scientific literature on µ-conotoxin research.
  • Analysis of studies mapping µ-conotoxin interactions with NaV channels.
  • Examination of structure-activity relationship data and species selectivity findings.

Main Results:

  • Detailed mapping of µ-conotoxin interactions across different NaV channel subtypes.
  • Elucidation of structure-activity relationships guiding conotoxin design.
  • Characterization of species-specific activity and the influence of disulfide bonds on function.

Conclusions:

  • Understanding µ-conotoxin interactions and structure is crucial for developing targeted analgesics.
  • Addressing subtype promiscuity is key to minimizing side effects.
  • Further research into disulfide connectivity can optimize conotoxin therapeutic potential.