@article{189381,
  keywords = {lasso peptides, molecular switches, Natural Products, rotaxane, supramolecular chemistry},
  author = {Hendrik V. Schr{\"o}der and Michael Stadlmeier and Martin W{\"u}hr and A. James Link},
  title = {The Shuttling Cascade in Lasso Peptide Benenodin-1 is Controlled by Non-Covalent Interactions},
  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 {\textquotedblleft}tail/loop pulling{\textquotedblright} 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{\textquoteright}s physico-chemical properties. },
  year = {2021},
  journal = {Chemistry {\textendash} A European Journal},
  url = {https://chemistry-europe.onlinelibrary.wiley.com/doi/abs/10.1002/chem.202103615},
  doi = {10.1002/chem.202103615},
  language = {eng},
}