Related Experiment Video
Updated: Jan 27, 2026

07:26
Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
13.4K
Assemblies of Peptides in a Complex Environment and their Applications
Huaimin Wang1, Zhaoqianqi Feng1, Bing Xu1
1Department of Chemistry, Brandeis University, 415 South St, Waltham, MA, 02454, USA.
Angewandte Chemie (International Ed. in English)
|March 24, 2019
Summary
Researchers are designing peptide assemblies for complex biological functions. This review covers advances in self-assembly, conformational control, and cellular applications, highlighting future potential.
Area of Science:
- Biochemistry and Materials Science
- Focuses on the intersection of peptide chemistry and biological applications.
Background:
- Peptide assemblies with emergent properties are gaining attention for complex functions.
- Research is expanding to design peptide assemblies for biological systems.
Purpose of the Study:
- To highlight recent developments in peptide assemblies and their biological applications.
- To discuss progress in designing peptides for controlled self-assembly.
- To emphasize spatiotemporal control of peptide assemblies in cellular contexts.
Main Methods:
- Review of recent literature on peptide assembly design and function.
- Discussion of conformational control in peptide self-assembly.
- Exploration of approach-instructed assembly for cellular applications.
Main Results:
- Peptide assemblies offer unique advantages for biological functions.
- Advances in rational design enable conformational control of peptide self-assembly.
- Spatiotemporal control of peptide assemblies is achievable in cellular environments.
Conclusions:
- Peptide assemblies show significant promise for advanced biological functions.
- Challenges remain in harnessing peptide assembly complexity for in vivo applications.
- Future research directions involve further exploration of rational design and cellular integration.
Related Concept Videos
Protein Complex Assembly
16.7K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.7K
Protein Complex Assembly
2.5K
2.5K
Assembly of Signaling Complexes
6.5K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.5K
Assembly of Complex Microtubule Structures
2.5K
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.
2.5K
Peptide Bonds
82.6K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
82.6K
Gene-Environment Interactions
1.1K
Gene expression is a dynamic process that is significantly influenced by environmental factors. This interaction underlies the complex nature of biological development and the phenotypic differences observed among individuals, even among those with identical genetic makeups. Factors such as radiation, temperature, behavior, nutrition, and stress play pivotal roles in determining how genes are expressed. The concept of the reaction range is central to understanding this interaction. It posits...
1.1K

