Related Experiment Video
Updated: Jul 5, 2026
07:49
Spontaneous Formation and Rearrangement of Artificial Lipid Nanotube Networks as a Bottom-Up Model for Endoplasmic Reticulum
Published on: January 22, 2019
Reversible transitions between peptide nanotubes and vesicle-like structures including theoretical modeling studies
Xuehai Yan1, Yue Cui, Qiang He
1Beijing National Laboratory for Molecular Sciences, International Joint Lab, Key Lab of Colloid and Interface Sciences, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100080 (PR China).
Chemistry (Weinheim an Der Bergstrasse, Germany)
|May 15, 2008
Summary
Peptide concentration controls the shape of self-assembling peptide nanostructures. Dilution forms vesicles, while concentration reforms nanotubes, enabling tunable morphology.
Area of Science:
- Supramolecular Chemistry
- Materials Science
- Nanotechnology
Background:
- Peptide-based self-assembling systems offer versatile applications.
- Peptide nanostructures exhibit environmental responsiveness.
- Controlling nanostructure morphology is crucial for tailored applications.
Purpose of the Study:
- To investigate the reversible shape transition of dipeptide nanotubes (DPNTs).
- To explore the influence of peptide concentration on nanostructure morphology.
- To develop a theoretical model for tunable self-assembly.
Main Methods:
- Utilized Scanning Electron Microscopy (SEM), Transmission Electron Microscopy (TEM), Atomic Force Microscopy (AFM), and Circular Dichroism (CD) spectroscopy.
- Investigated morphological changes induced by varying peptide concentrations.
- Developed a theoretical model to explain the observed shape transitions.
Main Results:
- Demonstrated a reversible shape transition between dipeptide nanotubes and vesicle-like structures.
- Observed that dilution of DPNT solutions leads to vesicle formation.
- Confirmed that concentrating the solution reassembles vesicles into nanotubes.
Conclusions:
- Peptide concentration is a key factor in controlling the morphology of self-assembled systems.
- The observed reversible transition allows for on-demand tuning of nanostructure shape.
- The theoretical model provides insights for designing novel self-assembling molecules with tunable morphologies.
Related Concept Videos
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...
00:59COP 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...
01:44Introduction to Membrane Traffic
The ER, Golgi apparatus, endosomes, and lysosomes work in tandem to modify, sort, and package proteins and lipids. An integrated membrane trafficking network facilitates the back and forth shuttling of molecules within different organelles in the same cell or across the cell membrane.
The transport of soluble and membrane proteins is mediated by transport vesicles that collect cargo from one cellular compartment and deliver it to another by fusing with the target organelle membrane. The Rab...
The transport of soluble and membrane proteins is mediated by transport vesicles that collect cargo from one cellular compartment and deliver it to another by fusing with the target organelle membrane. The Rab...