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Related Concept Videos

COP Coated Vesicles00:59

COP Coated Vesicles

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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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Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

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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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Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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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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Clathrin Coated Vesicles01:12

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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...
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Vesicular Tubular Clusters01:45

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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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Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

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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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Related Experiment Video

Updated: Sep 5, 2025

In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth
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In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth

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Peptide-Based Coacervate-Core Vesicles with Semipermeable Membranes.

Manzar Abbas1, Jack O Law2, Sushma N Grellscheid2,3

  • 1Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, Nijmegen, 6525 AJ, The Netherlands.

Advanced Materials (Deerfield Beach, Fla.)
|July 7, 2022
PubMed
Summary
This summary is machine-generated.

Tyrosine-rich peptide conjugates form stable, membrane-enclosed protocells. These artificial cells, stabilized by dityrosine cross-linking, offer potential for molecular crowding and drug delivery applications.

Keywords:
coacervate-core vesiclesenzyme compartmentalizationliquid-liquid phase separationmembranesprotocells

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Area of Science:

  • Biomimetic chemistry
  • Origins of life research
  • Synthetic biology

Background:

  • Coacervate droplets are potential protocell models but lack stable membranes and are prone to coalescence.
  • Existing protocell models struggle with stability and controlled interactions, hindering their development for advanced applications.

Purpose of the Study:

  • To develop stable, membrane-enclosed protocells from tyrosine-rich peptide conjugates.
  • To investigate the properties and potential applications of these novel protocell constructs.

Main Methods:

  • Liquid-liquid phase separation of tyrosine-rich peptide conjugates.
  • Enzymatic oxidation and cross-linking of peptides at the droplet interface.
  • Characterization of membrane properties using molecular weight cut-off determination and flicker spectroscopy.
  • Encapsulation of enzymes within protocells.

Main Results:

  • Formation of stable, membrane-enclosed protocells via enzymatic dityrosine cross-linking.
  • Creation of semipermeable membranes with tunable thickness and intrinsic fluorescence.
  • Demonstrated molecular weight cut-off of 2.5 kDa and low membrane bending rigidity (0.1kB T).
  • Successful encapsulation and functional activity of enzymes within the protocells.

Conclusions:

  • Tyrosine-rich peptide conjugates can form robust, membrane-bound protocells with tunable properties.
  • These protocells overcome limitations of simple coacervates, offering stability and controlled permeability.
  • The developed protocells show promise as artificial cells for molecular crowding, communication, and drug delivery systems.