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Related Concept Videos

Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

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Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
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The movement of ions like sodium, potassium, and calcium into and out of the cell is essential to maintain the electrochemical gradient in living cells. The ion channels—a class of membrane transport proteins—help maintain this ionic gradient for the smooth functioning of physiological activities such as maintaining cell size and volume, conducting nerve impulses, and gas and nutrient exchange.
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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.
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Assembly and Characterization of Biomolecular Memristors Consisting of Ion Channel-doped Lipid Membranes
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Biomimetic artificial ion channels based on beta-cyclodextrin.

Yassine El Ghoul1, Ruddy Renia, Ibrahima Faye

  • 1LAMBE, UMR8587, UEVE-CNRS-CEA, Bld François Mitterrand, 91025 Evry, France. cecile.huin@univ-evry.fr.

Chemical Communications (Cambridge, England)
|November 5, 2013
PubMed
Summary
This summary is machine-generated.

Star polymers with beta-cyclodextrin were synthesized using click chemistry. These polymers form stable, isolated pores in lipid bilayers, mimicking natural biological channels.

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Area of Science:

  • Supramolecular Chemistry
  • Polymer Science
  • Biophysical Chemistry

Background:

  • Biomimetic channels are crucial for understanding biological transport.
  • Controlling pore formation and stability in artificial systems remains a challenge.
  • Cyclodextrin-based materials offer unique host-guest properties for self-assembly.

Purpose of the Study:

  • To synthesize novel star polymers based on beta-cyclodextrin.
  • To investigate the self-assembly and pore-forming capabilities of these polymers in lipid bilayers.
  • To explore the potential of these synthetic pores as mimics of biological ion channels.

Main Methods:

  • Synthesis of star polymers utilizing "click-chemistry" (copper-catalyzed azide-alkyne cycloaddition).
  • Characterization of the synthesized polymers using Nuclear Magnetic Resonance (NMR) spectroscopy and Size Exclusion Chromatography (SEC).
  • Investigation of pore formation and aggregation behavior in lipid bilayers using Black Lipid Membrane (BLM) techniques.

Main Results:

  • Successful synthesis and characterization of beta-cyclodextrin-based star polymers.
  • Demonstration that triazole functional groups induce pH-dependent electrostatic hindrance.
  • Formation of well-defined, isolated unitary pores in lipid bilayers, preventing aggregation.
  • Observation of pore behavior that effectively mimics natural biological channels.

Conclusions:

  • Beta-cyclodextrin star polymers are effective building blocks for creating stable, artificial pores.
  • The pH-responsive electrostatic hindrance is key to controlling pore formation and preventing aggregation.
  • These synthetic pores show promise as biomimetic models for studying biological transport mechanisms.