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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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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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A "Plug-And-Display" Nanoparticle Vaccine Platform Based on Outer Membrane Vesicles Displaying SARS-CoV-2 Receptor-Binding Domain
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Antibiotic vesicles based on peptide-polymer complex coacervation.

Thomas Daniel Vogelaar1, Kuno Schwärzer2, Jan Skov Pedersen3

  • 1Department of Chemistry, University of Oslo, Postboks 1033 Blindern, 0315 Oslo, Norway.

Journal of Colloid and Interface Science
|November 20, 2025
PubMed
Summary
This summary is machine-generated.

Researchers developed novel complex coacervate core vesicles (C3Vs) for colistin delivery. These stable C3Vs enhance the therapeutic potential of colistin, a key antimicrobial peptide, while reducing its toxicity.

Keywords:
AntibioticsColistinComplex coacervateKineticsSelf-assemblySmall-angle scatteringVesicles

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Area of Science:

  • Materials Science
  • Biotechnology
  • Drug Delivery

Background:

  • Antimicrobial peptides (AMPs) show promise against multidrug-resistant bacteria.
  • Colistin, a potent AMP, has limited therapeutic use due to cytotoxicity and instability.
  • Complex coacervation is explored for advanced drug delivery platforms.

Purpose of the Study:

  • To investigate complex coacervate core vesicles (C3Vs) for colistin delivery.
  • To characterize C3V structure and stability using advanced scattering techniques.
  • To explore methods for enhancing colistin's therapeutic efficacy and reducing drawbacks.

Main Methods:

  • Formation of C3Vs by mixing cationic colistin with poly(ethylene oxide)-b-poly(methacrylic acid) (PEO-b-PMAA) diblock copolymers.
  • Preparation of C3Vs using protonated and deuterated PEO-b-PMAA.
  • Analysis using small-angle X-ray and neutron scattering (SAXS/SANS) with a tailored vesicle scattering model.

Main Results:

  • Detailed structural and compositional quantification of C3Vs for the first time.
  • Characterization of net-neutral vesicles (100-190 nm diameter) with consistent wall thickness (≈17-18 nm).
  • Observation of variable inner radius based on experimental conditions and formation of micelles at physiological ionic strength.
  • Demonstration of exceptional vesicle stability in salt-free solutions over 24 hours.

Conclusions:

  • Complex coacervate core vesicles (C3Vs) offer a promising platform for colistin delivery.
  • The study provides unprecedented structural insights into C3Vs, aiding future drug delivery system development.
  • C3Vs demonstrate potential for enhancing antimicrobial peptide therapeutics while mitigating limitations.