Related Experiment Video
Updated: Jun 7, 2026
07:10
In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth
Published on: June 28, 2019
Autocatalytic membrane-amplification on a pre-existing vesicular surface
Hiroshi Takahashi1, Yoshiyuki Kageyama, Kensuke Kurihara
1Graduate School of Arts and Sciences, The University of Tokyo, Komaba, Megro-ku, Tokyo 153-8902, Japan.
Chemical Communications (Cambridge, England)
|October 20, 2010
Summary
Anionic giant vesicles formed from phosphoric membrane molecules in water. These vesicles catalyzed their own growth, enabling self-replication using a scaffold mechanism for vesicle amplification.
Area of Science:
- Biomimetic chemistry
- Supramolecular chemistry
Background:
- The origin of life requires self-replicating systems.
- Giant vesicles are model systems for protocells.
Purpose of the Study:
- To investigate the self-assembly and autocatalytic growth of phosphoric membrane molecules.
- To explore vesicle self-replication mechanisms.
Main Methods:
- Observation of self-assembly in aqueous solution.
- Catalytic activity of vesicle surfaces.
- Scaffold-mediated vesicle formation.
Main Results:
- Phosphoric membrane molecules self-assembled into anionic giant vesicles.
- Vesicle surfaces catalyzed autocatalytic formation of membrane molecules.
- Amplified membrane molecules led to new vesicle formation using original vesicles as scaffolds.
Conclusions:
- Demonstrated a self-replicating system based on giant vesicle formation.
- Highlighted the potential role of such systems in the origin of life.
- Established a model for autocatalytic vesicle growth and amplification.
Related Concept Videos
01:12Clathrin 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...
01:45Vesicular 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...
With the help of motor proteins such...
01:32Pinching-off of Coated Vesicles
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...
01:26Fusion of Secretory Vesicles with the Plasma Membrane
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...
01:25Rab Cascades
Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
01:43SNAREs and Membrane Fusion
Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...