Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

11.6K
Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
11.6K
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

11.0K
Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
11.0K
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

2.5K
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...
2.5K
Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

8.6K
Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
8.6K
Resting Membrane Potential01:24

Resting Membrane Potential

19.3K
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...
19.3K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

A symmetric region produces a novel calcium binding mode in the human Cx46 connexon.

Protein science : a publication of the Protein Society·2026
Same author

A negative-hydrated constriction zone is revealed in the active state of the H<sub>v</sub>1 channel.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

From transporter to motor: Evolutionary and structural insights into the emergence of prestin's area-motor activity in mammals.

Protein science : a publication of the Protein Society·2026
Same author

Multiscale molecular dynamics simulations identify SNX-482/KV4.3 binding determinants.

Biophysical journal·2025
Same author

Regulation of voltage-sensing structures of CaV1.2 calcium channel by the auxiliary β3-subunit.

The Journal of general physiology·2025
Same author

3D-QSAR Design of New Bcr-Abl Inhibitors Based on Purine Scaffold and Cytotoxicity Studies on CML Cell Lines Sensitive and Resistant to Imatinib.

Pharmaceuticals (Basel, Switzerland)·2025

Related Experiment Video

Updated: Sep 7, 2025

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
10:53

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo

Published on: November 7, 2013

13.8K

Spider Toxin SNX-482 Gating Modifier Spontaneously Partitions in the Membrane Guided by Electrostatic Interactions.

Guido Mellado1,2, Nicolas Espinoza1,2,3, Jose Antonio Garate1,3,4

  • 1Centro Interdisciplinario de Neurociencias de Valparaíso, Facultad de Ciencias, Universidad de Valparaiso, Valparaiso 2362735, Chile.

Membranes
|June 23, 2022
PubMed
Summary

Spider toxin SNX-482 binds to calcium channels. Molecular simulations reveal it prefers negatively charged membranes, with binding driven by electrostatic interactions and membrane affinity, not just aqueous diffusion.

Keywords:
SNX-482calcium channelcysteine-rich peptidegating modifiermembrane partitioning

More Related Videos

Functional Evaluation of Biological Neurotoxins in Networked Cultures of Stem Cell-derived Central Nervous System Neurons
15:05

Functional Evaluation of Biological Neurotoxins in Networked Cultures of Stem Cell-derived Central Nervous System Neurons

Published on: February 5, 2015

9.5K
Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
08:55

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

9.7K

Related Experiment Videos

Last Updated: Sep 7, 2025

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
10:53

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo

Published on: November 7, 2013

13.8K
Functional Evaluation of Biological Neurotoxins in Networked Cultures of Stem Cell-derived Central Nervous System Neurons
15:05

Functional Evaluation of Biological Neurotoxins in Networked Cultures of Stem Cell-derived Central Nervous System Neurons

Published on: February 5, 2015

9.5K
Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
08:55

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

9.7K

Area of Science:

  • Biophysics
  • Molecular Pharmacology
  • Computational Biology

Background:

  • Spider toxin SNX-482 is a cysteine-rich peptide that modulates CaV2.3 calcium channel activity.
  • Cysteine-rich peptides bind to targets via aqueous phase diffusion or membrane lateral diffusion (reduction in dimensionality).

Purpose of the Study:

  • To investigate the binding mechanisms of SNX-482 to membranes with varying anionic compositions.
  • To explore the roles of electrostatics and diffusion in SNX-482 membrane interaction.

Main Methods:

  • Coarse-grained and atomistic molecular dynamics simulations.
  • Systematic study of SNX-482 partitioning with different anionic membrane compositions.
  • Diffusional analysis to differentiate binding mechanisms.

Main Results:

  • Identified a conserved protein patch on SNX-482 responsible for membrane insertion.
  • Demonstrated a preference for SNX-482 binding to partially negatively charged membranes.
  • Electrostatic interactions, specifically molecular dipole alignment, guide membrane binding.
  • Toxin diffusion along the membrane is significantly slower than in the aqueous phase.

Conclusions:

  • Membrane affinity, influenced by electrostatics and membrane charge, is the primary determinant of SNX-482 binding mechanism.
  • The findings suggest that SNX-482's interaction with CaV2.3 channels is critically dependent on its membrane association properties.