Metal–peptide rings form highly entangled topologically inequivalent frameworks with the same ring- and crossing-numbers

Tomohisa Sawada (), Ami Saito, Kenki Tamiya, Koya Shimokawa, Yutaro Hisada and Makoto Fujita ()
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Tomohisa Sawada: The University of Tokyo
Ami Saito: The University of Tokyo
Kenki Tamiya: The University of Tokyo
Koya Shimokawa: Saitama University
Yutaro Hisada: The University of Tokyo
Makoto Fujita: The University of Tokyo

Nature Communications, 2019, vol. 10, issue 1, 1-7

Abstract: Abstract With increasing ring-crossing number (c), knot theory predicts an exponential increase in the number of topologically different links of these interlocking structures, even for structures with the same ring number (n) and c. Here, we report the selective construction of two topologies of 12-crossing peptide [4]catenanes (n = 4, c = 12) from metal ions and pyridine-appended tripeptide ligands. Two of the 100 possible topologies for this structure are selectively created from related ligands in which only the tripeptide sequence is changed: one catenane has a T2-tetrahedral link and the other a three-crossed tetrahedral link. Crystallographic studies illustrate that a conformational difference in only one of the three peptide residues in the ligand causes the change in the structure of the final tetrahedral link. Our results thus reveal that peptide-based folding and assembly can be used for the facile bottom-up construction of 3D molecular objects containing polyhedral links.

Date: 2019
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DOI: 10.1038/s41467-019-08879-7

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