Related Experiment Video
Updated: May 19, 2026

07:26
Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Structural and conformational dynamics of self-assembling bioactive β-sheet peptide nanostructures decorated with
Sanghun Han1, Donghun Kim, So-hee Han
1Translational Research Center for Protein Function Control and Department of Materials Science & Engineering, Yonsei University, Seoul 120-749, Korea.
Journal of the American Chemical Society
|September 4, 2012
Summary
Bioactive peptide nanostructures exhibit dynamic shell mobility and a stable core. Their structure responds to environmental changes, offering insights for designing responsive nanomaterials.
Area of Science:
- Biomaterials Science
- Nanotechnology
- Biophysics
Background:
- Understanding nanomaterial dynamics is crucial for developing controllable, tailor-made materials, especially for biological applications.
- Biomolecules are inherently dynamic and responsive to external stimuli, necessitating dynamic studies of nanostructures.
Purpose of the Study:
- To investigate the structural and conformational dynamics of self-assembling bioactive β-sheet peptide nanostructures.
- To elucidate the relationship between the bioactive peptide shell and the β-ribbon core dynamics.
Main Methods:
- Electron Paramagnetic Resonance (EPR) spectroscopy was employed to study the dynamics.
- Model peptide nanostructures with a cross-β spine and bioactive peptide shell were characterized.
Main Results:
- Bioactive peptides in the shell showed mobility similar to isolated monomers.
- The cross-β spine periphery was less mobile than the surface-displayed peptides.
- Fibril dynamics were independent of aggregation length, with shell peptides responding first to environmental changes.
Conclusions:
- The cross-β spine exhibits environmental resistance, with abrupt disintegration upon significant perturbation.
- These findings provide a comprehensive understanding of β-sheet peptide nanostructure dynamics.
- The results are valuable for the design of dynamic, self-assembled peptide nanostructures for various applications.
Related Concept Videos
Protein Folding
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Overview
Protein Organization
Overview
Protein Organization
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
The primary structure of a protein is its amino acid sequence.
Protein Complex Assembly
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...
Nucleic Acid Structure
The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms a 5′ to 3′ phosphodiester linkage.
DNA Structure
DNA has a double-helix structure. The...
DNA Structure
DNA has a double-helix structure. The...

