ArticleChemistry (Weinheim an der Bergstrasse, Germany)2022
The Shuttling Cascade in Lasso Peptide Benenodin-1 is Controlled by Non-Covalent Interactions.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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Who cites it
4 citing papers in PubMed.
- Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026Review
- Lasso Peptide Syanodin I: Loop-Pulling Two-Step Thermal Unthreading Mechanism.Analytical chemistry · 2025Article
- In silico design of foldable lasso peptides.Biophysical journal · 2025Article
- Switchable protection and exposure of a sensitive squaraine dye within a redox active rotaxane.Communications chemistry · 2024Article
Corrections and comments
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Authors and funding
4 authors.
Funding
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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Registered trials
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