Related Experiment Video
Updated: Jul 1, 2026

07:26
Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Aggregation and columnar assembly of crescent oligoamides
Yunfeng Zhang1, Kazuhiro Yamato, Kai Zhong
1Chengdu Institute of Organic Chemistry, Chinese Academy of Sciences, Chengdu, 610041, China.
Organic Letters
|September 12, 2008
Summary
Oligoamide molecules with up to six benzene rings form large aggregates in solution and self-assemble into columnar structures in the solid state, creating potential channels.
Area of Science:
- Supramolecular chemistry
- Organic materials science
- Crystal engineering
Background:
- Oligoamides are versatile molecular building blocks.
- Understanding their self-assembly is crucial for materials design.
- Crescent-shaped oligoamides present unique structural possibilities.
Purpose of the Study:
- To investigate the aggregation and assembly behavior of crescent oligoamides.
- To characterize the solid-state structures formed by these molecules.
- To explore the potential for channel formation in the assembled structures.
Main Methods:
- Synthesis and characterization of oligoamides with 2-6 benzene residues.
- Solution-state aggregation studies (e.g., in chloroform).
- Solid-state structural analysis using X-ray diffraction (single crystal and powder).
Main Results:
- Pentamer and hexamer oligoamides form large aggregates in chloroform.
- All investigated oligoamides self-assemble into columnar structures in the solid state.
- These columnar assemblies are driven by stacking interactions.
- Columnar assemblies of pentamer and hexamer oligoamides are predicted to form hydrophilic channels.
Conclusions:
- Crescent oligoamides exhibit concentration- and state-dependent aggregation.
- Solid-state self-assembly leads to ordered columnar structures.
- The potential for hydrophilic channels in pentamer and hexamer assemblies offers opportunities for applications in separation or transport.
Related Concept Videos
Oligosaccharide Assembly
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...
Assembly of Cytoskeletal Filaments
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
Golgi Matrix Proteins
Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Formation of Higher-order Actin Filaments
The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin networks...
The high-order actin networks...
Assembly of Complex Microtubule Structures
Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.

