Related Experiment Video
Updated: Jan 15, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
From Monomers to Nanocapsules: The Role of Structural Features in Amino-Acid-Derived BTA Self-Assembly
Anna Walczak1,2, Grzegorz Markiewicz1,2, Michał Gliński1,2
1Centre for Advanced Technologies, Adam Mickiewicz University in Poznań, Uniwersytetu Poznańskiego 10, Poznań 61-614, Poland.
Abstract:
The morphology of supramolecular assemblies can be profoundly influenced by even subtle changes in the molecular structure. In this study, we investigate how variations in amino acid-functionalized benzene-1,3,5-tricarboxamide (BTA) derivatives affect their self-assembly behavior in nonpolar solvents. Specifically, we examine the roles of linker flexibility, steric hindrance introduced by bulky substituents at the 2,4,6-positions, and the nature of the central core (aromatic vs aliphatic). Our results show that these structural changes lead to strikingly different aggregation outcomes, ranging from monomeric species and ill-defined oligomers to well-defined nanocapsules. These findings highlight the importance of precise molecular design in controlling supramolecular self-assembly and demonstrate how specific structural factors dictate the morphology and properties of the resulting materials.
Related Concept Videos
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Organization
Protein Organization
The primary structure of a protein is its amino acid sequence....
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Assembly of Cytoskeletal Filaments

