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Updated: Oct 12, 2025

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
Published on: February 6, 2020
The Shuttling Cascade in Lasso Peptide Benenodin-1 is Controlled by Non-Covalent Interactions
Hendrik V Schröder1, Michael Stadlmeier2, Martin Wühr2
1Department of Chemical and Biological Engineering, Princeton University, Princeton, NJ, 08544, USA.
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.
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