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Related Concept Videos

Membrane Fluidity01:26

Membrane Fluidity

Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is a relatively...
Membrane Fluidity01:23

Membrane Fluidity

Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.Fatty acids tails of phospholipids can be either saturated or...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

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...

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Related Experiment Video

Updated: Jul 9, 2026

Phase Behavior of Charged Vesicles Under Symmetric and Asymmetric Solution Conditions Monitored with Fluorescence Microscopy
10:08

Phase Behavior of Charged Vesicles Under Symmetric and Asymmetric Solution Conditions Monitored with Fluorescence Microscopy

Published on: October 24, 2017

Adhesion of fluid vesicles at chemically structured substrates.

G T Linke1, R Lipowsky, T Gruhn

  • 1Max Planck Institute of Colloids and Interfaces, Science Park Golm, D-14424 Potsdam, Germany.

The European Physical Journal. E, Soft Matter
|November 30, 2007
PubMed
Summary

Fluid vesicles adhere to structured substrates, with adhesion restricted by attractive domain size. Vesicle shape and contact area depend on domain characteristics and osmotic pressure.

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Obtention of Giant Unilamellar Hybrid Vesicles by Electroformation and Measurement of their Mechanical Properties by Micropipette Aspiration

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Last Updated: Jul 9, 2026

Phase Behavior of Charged Vesicles Under Symmetric and Asymmetric Solution Conditions Monitored with Fluorescence Microscopy
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Phase Behavior of Charged Vesicles Under Symmetric and Asymmetric Solution Conditions Monitored with Fluorescence Microscopy

Published on: October 24, 2017

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Obtention of Giant Unilamellar Hybrid Vesicles by Electroformation and Measurement of their Mechanical Properties by Micropipette Aspiration
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Obtention of Giant Unilamellar Hybrid Vesicles by Electroformation and Measurement of their Mechanical Properties by Micropipette Aspiration

Published on: January 19, 2020

Area of Science:

  • Biophysics
  • Soft Matter Physics
  • Computational Biology

Background:

  • Understanding vesicle adhesion to surfaces is crucial for biological processes and nanotechnology.
  • Chemically patterned substrates offer precise control over cell and vesicle interactions.
  • Previous studies often simplified substrate interactions or vesicle properties.

Purpose of the Study:

  • To theoretically investigate fluid vesicle adhesion to chemically structured substrates.
  • To determine how substrate domain geometry and properties influence vesicle adhesion and morphology.
  • To explore the role of membrane tension and bending rigidity in vesicle-substrate interactions.

Main Methods:

  • Monte Carlo simulations were employed to model vesicle-substrate interactions.
  • A planar substrate with a single attractive domain (gamma) was simulated.
  • Vesicle size, domain size, adhesion strength, and bending rigidity were varied.

Main Results:

  • Vesicle spreading is limited by the size of the attractive domain.
  • At domain boundaries, low membrane tension and shape fluctuations (governed by bending rigidity) occur.
  • For circular domains, membrane oscillations around a spherical cap shape were observed.
  • Contact area changes with osmotic pressure depending on vesicle and domain size.
  • Optimal lateral localization of the vesicle's center of mass occurs at a specific domain radius.
  • Contact area width on stripe domains varies nonmonotonically with adhesion strength.

Conclusions:

  • Substrate domain geometry significantly dictates vesicle adhesion dynamics and morphology.
  • Membrane properties like bending rigidity play a key role in shape fluctuations during adhesion.
  • The findings provide insights into controlling vesicle-substrate interactions for potential applications.