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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 "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.

SUBMITTER: Schroder HV

PROVIDER: S-EPMC8792204 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature

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

Schröder Hendrik V HV Stadlmeier Michael M Wühr Martin M Link A James AJ

Chemistry (Weinheim an der Bergstrasse, Germany) 20211202 5

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. F ...[more]

PMID: 34797593

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