Related Experiment Video
Updated: Oct 18, 2025

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Metal-Peptide Nonafoil Knots and Decafoil Supercoils
Yuuki Inomata1, Tomohisa Sawada1,2, Makoto Fujita1,3
1Department of Applied Chemistry, School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.
Abstract:
Despite the frequent occurrence of knotted frameworks in protein structures, the latent potential of peptide strands to form entangled structures is rarely discussed in peptide chemistry. Here we report the construction of highly entangled molecular topologies from Ag(I) ions and tripeptide ligands. The efficient entanglement of metal-peptide strands and the wide scope for design of the amino acid side chains in these ligands enabled the construction of metal-peptide 91 torus knots and 1012 torus links. Moreover, steric control of the peptide side chain induced ring opening and twisting of the torus framework, which resulted in an infinite toroidal supercoil nanostructure.
Related Concept Videos
Protein Folding
Protein Organization
Peptide Bonds
Fibrous Proteins
Protein-protein Interfaces
DNA Topoisomerases
Types and Mechanism of action
Topoisomerases are divided into two main types. ...

