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Biomaterials

Macrocycle folds up like a protein

Hydrogen bonds and π-stacking interactions hold compact, twisted structure in place

by Celia Arnaud
January 7, 2019 | A version of this story appeared in Volume 97, Issue 1

 

A stick structure of a macrocyclic foldamer, with one of its stacks of three aromatic rings and capping adenines highlighted.
Credit: J. Am. Chem. Soc.
This 15-subunit macrocycle folds up like a protein. Its five stacks of aromatic rings (shown as space-filling, left and right) are capped with adenine at both ends.

Biological macromolecules such as proteins and nucleic acids can fold into complex shapes with well-defined architectures. A team led by Sijbren Otto of the University of Groningen, in collaboration with Ennio Zangrando of the University of Trieste and Piotr J. Chmielewski of the University of Wrocław, has now identified a small molecule that folds in a similar way to a protein, spontaneously assembling into a macrocycle called a foldamer (J. Am. Chem. Soc. 2018, DOI: 10.1021/jacs.8b11698). The building block consists of a nucleobase attached to an amino acid. At a concentration of ~500 µM, it assembles into a 15-subunit macrocycle that folds into a compact structure held in place by hydrogen bonds and π-stacking interactions. It has a highly twisted conformation, including five stacks of three aromatic rings, each stack capped with adenine rings. The spontaneous transition from small molecule to folded macromolecule is unusual, says Samuel H. Gellman, an expert on foldamers at the University of Wisconsin–Madison. “The discovery itself will stimulate others to consider new ways to explore the mystery of biomacromolecule development.”

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