The Shuttling Cascade in Lasso Peptide Benenodin-1 is Controlled by Non-Covalent Interactions

Hendrik V. Schröder, Michael Stadlmeier, Martin Wühr, Aaron James Link

Research output: Contribution to journalArticlepeer-review

Abstract

The lasso peptide benenodin-1, a naturally occurring and bacterially produced [1]rotaxane, undergoes a reversible zip tie-like motion under heat activation, in which a peptidic wheel stepwise translates along a molecular thread in a cascade of “tail/loop pulling” equilibria. Conformational and structural analyses of four translational isomers, in solution and in the gas phase, reveal that the equilibrium distribution is controlled by mechanical and non-covalent forces within the lasso peptide. Furthermore, each dynamic pulling step is accompanied by a major restructuring of the intramolecular hydrogen bonding network between wheel and thread, which affects the peptide's physico-chemical properties.

Original languageEnglish (US)
JournalChemistry - A European Journal
DOIs
StateAccepted/In press - 2021

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Organic Chemistry

Keywords

  • lasso peptides
  • molecular switches
  • natural products
  • rotaxane
  • supramolecular chemistry

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