Lipid-Head-Polymer-Tail Chimeric Vesicles
Kan Hu1, Aoyuan Cheng1, Dingcheng Zhou1
1Hefei National Laboratory for Physical Sciences at the Microscale, University of Science and Technology of China, Hefei, 230026, China.
Macromolecular Rapid Communications
|July 8, 2022
Summary
Researchers developed novel chimeric nanovesicles (CNVs) by combining lipids and polymers. These advanced nanocarriers offer improved stability and reduced permeability, showing promise for drug delivery applications.
Area of Science:
- Biomaterials Science
- Nanotechnology
- Drug Delivery Systems
Background:
- Lipid nanovesicles (LNVs) and polymer nanovesicles (PNVs) are crucial for global health but have limitations.
- LNVs (liposomes) and PNVs (polymersomes) face challenges in permeability and protein interaction, respectively.
Purpose of the Study:
- To synthesize and characterize novel chimeric nanovesicles (CNVs) by covalently linking lipid and polymer components.
- To evaluate the potential of CNVs as advanced nanocarriers for therapeutic molecules.
Main Methods:
- Facile ring-opening polymerization to create CNVs from a phosphate lipid head and polylactide polymer tail.
- Synthesis conducted on a 500 g scale.
- In vitro delivery experiments using fluorescein-PEG, rhodamine-PEG, and doxorubicin.
Main Results:
- CNVs demonstrated reduced permeability for both small and large molecules compared to LNVs.
- CNVs exhibited enhanced tolerance toward proteins in buffer solutions, unlike conventional PNVs requiring PEGylation.
- Successful in vitro delivery of model molecules and doxorubicin confirmed CNV efficacy.
Conclusions:
- Chimeric nanovesicles represent a promising new class of nanomaterials for drug delivery.
- CNVs overcome limitations of traditional LNVs and PNVs, offering improved stability and biocompatibility.
- These nanocarriers hold significant potential for translational nanomedicine applications.
Related Concept Videos
Intralumenal Vesicles and Multivesicular Bodies
3.7K
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...
3.7K
Clathrin Coated Vesicles
7.2K
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...
7.2K
Fusion of Secretory Vesicles with the Plasma Membrane
11.5K
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.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
11.5K
COP Coated Vesicles
8.0K
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...
8.0K
Tail-anchoring of Proteins in the ER Membrane
3.2K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
3.2K


