Related Experiment Video
Updated: Jun 12, 2025

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Boosting stability: a hierarchical approach for self-assembling peptide structures
Denys Balandin1,2, Natalia Szulc3, Dominika Bystranowska4
1Department of Bioorganic Chemistry, Faculty of Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, Wrocław 50-370, Poland. monika.szefczyk@pwr.edu.pl.
Abstract:
The primary objective of this study was to implement a hierarchical approach to enhance the conformational stability of a selected group of peptides by incorporating trans-(1S,2S)-2-aminocyclopentanecarboxylic acid (trans-ACPC). The influence of residue mutation on the peptide structures was investigated using circular dichroism, analytical ultracentrifugation, and vibrational spectroscopy. The resulting nanostructures were examined via transmission electron microscopy. The incorporation of trans-ACPC led to increased conformational stability and self-assembling propensity in peptides containing constrained β-amino acid residues.
Related Concept Videos
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Organization
The primary structure of a protein is its amino acid sequence....
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme...
Molecular Chaperones and Protein Folding
The...
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...

