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Biomimetic chemistry

Ribosome tolerates artificial foldamers

München, 03/22/2018

Schematic view of a foldamer-peptide hybrid emerging from the ribosome’s exit tunnel. The aromatic foldamer (in yellow) is helically folded whereas the peptide (in green) has not yet fully come out of the ribosome. (Credit: Dr. Sunbum Kown)

Chemist Ivan Huc creates artificial folded molecular architectures called ‘foldamers’. In a publication that has just appeared in Nature Chemistry and is featured on the cover of the April issue, he shows that cellular ribosomes tolerate some foldamers during synthesis, and can both produce both noncyclic and cyclic foldamer-peptide hybrid molecules.

The new paper builds on advances described in a previous publication in Nature Chemistry, which was published earlier this year. In this paper, Huc and his colleagues developed a pattern of binding interactions required to enable synthetic molecules to assume stable forms similar to the helical backbones of proteins. (Nature Chemistry 2018)