An artificial molecular machine that builds an asymmetric catalyst

Research output: Contribution to journalArticle

  • External authors:
  • Malcolm A.Y. Gall
  • Sonja Kuschel
  • Julien De Winter
  • Pascal Gerbaux

Abstract

Biomolecular machines perform types of complex molecular-level tasks that artificial molecular machines can aspire to. The ribosome, for example, translates information from the polymer track it traverses (messenger RNA) to the new polymer it constructs (a polypeptide) 1 . The sequence and number of codons read determines the sequence and number of building blocks incorporated into the biomachine-synthesized polymer. However, neither control of sequence 2,3 nor the transfer of length information from one polymer to another (which to date has only been accomplished in man-made systems through template synthesis) 4 is easily achieved in the synthesis of artificial macromolecules. Rotaxane-based molecular machines 5-7 have been developed that successively add amino acids 8-10 (including β-amino acids 10 ) to a growing peptide chain by the action of a macrocycle moving along a mono-dispersed oligomeric track derivatized with amino-acid phenol esters. The threaded macrocycle picks up groups that block its path and links them through successive native chemical ligation reactions 11 to form a peptide sequence corresponding to the order of the building blocks on the track. Here, we show that as an alternative to translating sequence information, a rotaxane molecular machine can transfer the narrow polydispersity of a leucine-ester-derivatized polystyrene chain synthesized by atom transfer radical polymerization 12 to a molecular-machine-made homo-leucine oligomer. The resulting narrow-molecular-weight oligomer folds to an α-helical secondary structure 13 that acts as an asymmetric catalyst for the Juliá-Colonna epoxidation 14,15 of chalcones.

Bibliographical metadata

Original languageEnglish
Pages (from-to)381-385
Number of pages5
JournalNature Nanotechnology
Volume13
Issue number5
Early online date2 Apr 2018
DOIs
Publication statusPublished - 1 May 2018

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