Related Experiment Video
Updated: Sep 20, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Biomimetic organization: Octapeptide self-assembly into nanotubes of viral capsid-like dimension
Céline Valéry1, Maïté Paternostre, Bruno Robert
1Unité Mixte de Recherche 8612, Centre National de la Recherche Scientifique, Faculté de Pharmacie, 5 Rue J.B. Clément, 92296 Châtenay-Malabry Cedex, France.
Abstract:
The controlled self-assembly of complex molecules into well defined hierarchical structures is a promising route for fabricating nanostructures. These nanoscale structures can be realized by naturally occurring proteins such as tobacco mosaic virus, capsid proteins, tubulin, actin, etc. Here, we report a simple alternative method based on self-assembling nanotubes formed by a synthetic therapeutic octapeptide, Lanreotide in water. We used a multidisciplinary approach involving optical and electron microscopies, vibrational spectroscopies, and small and wide angle x-ray scattering to elucidate the hierarchy of structures exhibited by this system. The results revealed the hexagonal packing of nanotubes, and high degree of monodispersity in the tube diameter (244 A) and wall thickness (approximately equal to 18 A). Moreover, the diameter is tunable by suitable modifications in the molecular structure. The self-assembly of the nanotubes occurs through the association of beta-sheets driven by amphiphilicity and a systematic aromatic/aliphatic side chain segregation. This original and simple system is a unique example for the study of complex self-assembling processes generated by de novo molecules or amyloid peptides.
Related Concept Videos
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Viral Structure
Assembly of Cytoskeletal Filaments
Size and Structure of Viral Genomes
Assembly of Complex Microtubule Structures
Protein Organization

