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Related Concept Videos

Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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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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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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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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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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Pinching-off of Coated Vesicles01:32

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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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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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Related Experiment Video

Updated: Apr 19, 2026

Solubility of Hydrophobic Compounds in Aqueous Solution Using Combinations of Self-assembling Peptide and Amino Acid
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Functional vesicles formed by anticancer drug assembly.

Wenjun Zhu1, Shuo Fang1, Yemin Zhang1

  • 1School of Chemistry and Chemical Engineering, Southeast University, Nanjing 210096, China.

Bioorganic & Medicinal Chemistry Letters
|December 18, 2014
PubMed
Summary
This summary is machine-generated.

Researchers developed novel nitrogen mustard conjugate vesicles for enhanced anticancer drug delivery. These stable vesicles show comparable efficacy to the parent drug, offering potential for improved cancer treatments.

Keywords:
Antitumor activityConjugateNitrogen mustardsPeptideSelf-assembly

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Area of Science:

  • Medicinal Chemistry
  • Nanotechnology
  • Oncology

Background:

  • Nitrogen mustards are effective anticancer agents but often suffer from poor stability and efficiency.
  • Developing novel drug delivery systems can overcome limitations of conventional chemotherapeutics.

Purpose of the Study:

  • To design and synthesize a new nitrogen mustard conjugate self-assembling into stable vesicles.
  • To evaluate the stability, self-assembly characteristics, and in vitro antitumor activity of the novel conjugate vesicles.

Main Methods:

  • Synthesis of benzoic acid nitrogen mustard-peptide (AAAK) conjugate.
  • Characterization of vesicle formation using dynamic light scattering (DLS), transmission electron microscopy (TEM), and circular dichroism (CD).
  • Assessment of conjugate vesicle stability in aqueous solution and in vitro antitumor activity via MTT assay against cancer cell lines (MCF-7, Hela, HepG-2).

Main Results:

  • The benzoic acid nitrogen mustard-peptide (AAAK) conjugate successfully self-assembled into vesicles in water.
  • Vesicle formation was confirmed by DLS, TEM, and CD analyses.
  • The conjugate vesicles exhibited enhanced stability in aqueous solution compared to the parent drug.
  • In vitro studies demonstrated comparable antitumor activity of the free drug conjugate to the parent drug against tested cancer cell lines.

Conclusions:

  • Benzoic acid nitrogen mustard-peptide (AAAK) conjugate vesicles represent a promising new drug delivery system.
  • The developed vesicles offer improved stability and maintain significant antitumor efficacy.
  • This novel approach holds potential for advancing cancer therapy through enhanced drug delivery.