Related Experiment Video
Updated: Jun 14, 2026
10:01
Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
Published on: April 8, 2020
DNA-mediated self-assembly of artificial vesicles
Maik Hadorn1, Peter Eggenberger Hotz
1Artificial Intelligence Laboratory, Department of Informatics, University of Zurich, Zurich, Switzerland. hadorn@ifi.uzh.ch
Plos One
|April 3, 2010
Summary
Researchers developed a novel DNA-linker system for creating stable, multicompartment vesicles. This breakthrough enables precise control over vesicle assembly for advanced applications in analysis, synthesis, and personalized medicine.
Area of Science:
- Biotechnology
- Materials Science
- Nanotechnology
Background:
- Current multicompartment vesicle systems are limited by binary tethering protocols.
- Existing methods for creating distinct vesicle populations lack specificity and require complex readjustments.
Purpose of the Study:
- To develop a robust method for creating stable multicompartment vesicle systems.
- To overcome limitations of current tethering protocols for vesicle assembly.
Main Methods:
- Utilized biotinylated DNA single strands as linkers.
- Anchored DNA linkers to phospholipid-grafted biotinylated polyethylene glycol (PEG) tethers.
- Employed streptavidin as a connector for vesicle-vesicle self-assembly.
Main Results:
- Demonstrated successful incorporation of PEG tethers into vesicle membranes during formation.
- Confirmed specific anchoring sites for streptavidin loading.
- Established that DNA-mediated vesicle self-assembly is sequence-dependent and influenced by monovalent salts.
Conclusions:
- Provides a foundation for advanced multi-vesicle assemblies.
- Facilitates complex bottom-up systems for analysis and synthesis.
- Enables potential applications in personalized medicine through targeted drug delivery.
Related Concept Videos
02:41Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
01:32Pinching-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...
01:38Intralumenal Vesicles and Multivesicular Bodies
Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
01:43SNAREs 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...
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...
01:12Clathrin 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...
01:26Fusion of Secretory Vesicles with the Plasma Membrane
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...