Related Experiment Video
Updated: Dec 23, 2025

09:48
Investigating Single Molecule Adhesion by Atomic Force Spectroscopy
Published on: February 27, 2015
10.7K
Vesicle adhesion in the electrostatic strong-coupling regime studied by time-resolved small-angle X-ray scattering
Karlo Komorowski1, Jannis Schaeper1, Michael Sztucki2
1Institute for X-Ray Physics, University of Göttingen, Friedrich-Hund-Platz 1, 37077 Göttingen, Germany. tsaldit@gwdg.de.
Soft Matter
|April 23, 2020
Summary
Divalent ions induce lipid vesicle adhesion, with results aligning with strong coupling theory. Highly charged bilayers show transient adhesion before forming multilamellar structures.
Area of Science:
- Biophysics
- Materials Science
- Physical Chemistry
Background:
- Lipid vesicle adhesion is crucial for biological processes.
- Electrostatic interactions, particularly with divalent ions, significantly influence membrane behavior.
- Understanding ion-mediated vesicle interactions is key to deciphering cellular functions.
Purpose of the Study:
- To investigate lipid vesicle adhesion in the electrostatic strong-coupling regime induced by divalent ions.
- To explore the influence of surface charge density and ion type on vesicle adhesion and bilayer structure.
- To examine the dynamic nature of adhesion and subsequent structural transformations.
Main Methods:
- Time-resolved small-angle X-ray scattering (SAXS) was employed to study vesicle adhesion.
- Stopped-flow rapid mixing technique was combined with SAXS for dynamic measurements.
- Vesicles composed of varying DOPC:DOPS mixtures were analyzed with different divalent ions (Ca2+, Sr2+, Zn2+).
Main Results:
- Adhesion and interbilayer distances (dw) were measured for different lipid compositions and ions.
- Results showed good agreement with strong coupling theory, including ion-correlation-based like-charge attraction.
- Highly charged bilayers exhibited transient adhesion, followed by transformation into multilamellar vesicle phases.
Conclusions:
- Divalent ions effectively induce lipid vesicle adhesion via strong electrostatic coupling.
- The observed adhesion and subsequent transformations are consistent with theoretical predictions.
- Microfluidic environments show promise for future advanced SAXS studies of vesicle dynamics.
Related Concept Videos
Pinching-off of Coated Vesicles
3.9K
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...
3.9K
COP Coated Vesicles
16.7K
Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of...
16.7K
Fusion of Secretory Vesicles with the Plasma Membrane
16.4K
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...
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
16.4K
Vesicular Tubular Clusters
3.0K
After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
With the help of motor proteins such...
3.0K
Clathrin Coated Vesicles
8.8K
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...
8.8K
Studying the Cytoskeleton
8.4K
The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
8.4K

