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Related Concept Videos

COP Coated Vesicles00:59

COP Coated Vesicles

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 different...
Clathrin Coated Vesicles01:12

Clathrin 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...
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
ER Retrieval Pathway01:45

ER Retrieval Pathway

In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...

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Related Experiment Video

Updated: Jul 7, 2026

In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth
07:10

In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth

Published on: June 28, 2019

Sequence-Defined Short Peptide-Derived Coacervate Vesicles for Targeted Therapeutics.

Sandip Sarkar1, Rajsekhar Roy2, Atin Chatterjee1

  • 1Department of Chemical Sciences and Center for Advanced Functional Materials, Indian Institute of Science Education and Research (IISER) Kolkata, Mohanpur, West Bengal, India.

Advanced Materials (Deerfield Beach, Fla.)
|July 6, 2026
PubMed
Summary

A novel peptide forms stable, enzyme-responsive coacervate vesicles (CVs) for targeted cancer therapy. These vesicles release therapeutic cargo upon encountering tumor enzymes, triggering a cascade that suppresses tumor growth.

Keywords:
Alkaline phosphatase (ALP) responsivenessCancer therapyCoacervate vesicles (CVs)Liquid–Liquid Phase Separation (LLPS)Peptide CoacervatesStimuli‐responsiveSupramolecular Transformation

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Delivery of Therapeutic siRNA to the CNS Using Cationic and Anionic Liposomes

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Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
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Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro

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Last Updated: Jul 7, 2026

In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth
07:10

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Published on: June 28, 2019

Delivery of Therapeutic siRNA to the CNS Using Cationic and Anionic Liposomes
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Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
10:01

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro

Published on: April 8, 2020

Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Chemical Biology

Background:

  • Compartmentalization is crucial for biological organization and developing advanced therapeutic carriers.
  • Programmable delivery systems require precise control over molecular assembly and release.

Purpose of the Study:

  • To design a sequence-defined peptide capable of forming stable, enzyme-responsive coacervate vesicles (CVs) for targeted cancer therapy.
  • To investigate the therapeutic potential of these CVs through a synergistic cascade involving enzymatic starvation, oxidative stress, and nitric oxide (NO) generation.

Main Methods:

  • Synthesis of a sequence-defined peptide (Biotin-SR) with pH-responsive and enzyme-cleavable functionalities.
  • Formation of lipid-free coacervate vesicles (CVs) via liquid-liquid phase separation.
  • Encapsulation of glucose oxidase (GOx) and assessment of cargo release triggered by alkaline phosphatase (ALP).
  • In vitro and in vivo evaluation of therapeutic efficacy in cancer models.

Main Results:

  • Biotin-SR peptides formed structurally persistent, lipid-free coacervate vesicles (CVs) through liquid-liquid phase separation.
  • The CVs demonstrated selective targeting of cancer cells via biotin-mediated recognition.
  • Enzymatic dephosphorylation by ALP in tumor environments triggered irreversible charge loss, GOx release, and a synergistic therapeutic cascade.
  • The combined effects of glucose depletion and NO generation led to elevated reactive oxygen species (ROS), mitochondrial dysfunction, and suppressed tumor growth.

Conclusions:

  • Minimal peptide sequences can be engineered to create stable coacervate vesicles with enzyme-responsive supramolecular functions.
  • This approach enables targeted delivery and triggered release of therapeutics, leading to synergistic anticancer effects.
  • The developed peptide-based CVs represent a promising platform for advanced, programmable therapeutic carriers.