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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...
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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...
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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...
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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.
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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.
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Updated: Oct 15, 2025

A Facile and Efficient Approach for the Production of Reversible Disulfide Cross-linked Micelles
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Dendrimer-Based Polyion Complex Vesicles: Loops Make Loose.

Jianan Huang1, Chendan Li1, Yifan Gao1

  • 1Shanghai Key Laboratory of Multiphase Materials Chemical Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, P. R. China.

Macromolecular Rapid Communications
|October 26, 2021
PubMed
Summary
This summary is machine-generated.

Polymer self-assembly can be kinetically controlled, yielding distinct structures like micelles and vesicles. This kinetic control offers a pathway to create functional nanoparticles with tunable properties for specific applications.

Keywords:
PAMAMsdynamicsloopspolyion complex vesiclestriblock copolymers

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Area of Science:

  • Polymer science
  • Supramolecular chemistry
  • Materials science

Background:

  • Amphiphile self-assembly is typically governed by thermodynamic control via the packing parameter.
  • The ability of polymers to relax and reach thermodynamic equilibrium is not always guaranteed.
  • Kinetic control offers an alternative mechanism for directing self-assembly.

Purpose of the Study:

  • To investigate the role of kinetic control in polyion complex (PIC) assembly.
  • To explore the formation of different morphologies (micelles and vesicles) from block copolymers and dendrimers.
  • To understand the influence of precursor complex dynamics on final structure and properties.

Main Methods:

  • Combining poly(ethylene oxide)-b-(styrene sulfonate) (PEO-PSS) block copolymers with cationic polyamidoamine (PAMAM) dendrimers of varying generations.
  • Characterizing the self-assembled structures (micelles and vesicles) using relevant techniques.
  • Assessing the stability and dynamics of the assemblies in response to salt concentration and time.

Main Results:

  • Diblocks and triblocks with similar packing parameters formed distinct structures: core-shell micelles and vesicles, respectively.
  • Micelles exhibited high salt stability, while vesicles were salt-sensitive and showed dynamic matter exchange.
  • Small, kinetically trapped precursor complexes were identified as the cause of morphological and dynamic differences.

Conclusions:

  • Kinetic control of PIC assembly can yield particles with well-defined and useful properties.
  • Triblock copolymers form more dynamic vesicles, suggesting potential for "active" nanomaterials.
  • This work opens new avenues for tuning PICsomes for targeted applications through kinetic pathways.