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

TitleThe Shuttling Cascade in Lasso Peptide Benenodin-1 is Controlled by Non-Covalent Interactions.
Publication TypeJournal Article
Year of Publication2022
AuthorsSchröder, HV, Stadlmeier, M, Wühr, M, A Link, J
JournalChemistry
Volume28
Issue5
Paginatione202103615
Date Published2022 Jan 24
ISSN1521-3765
KeywordsHydrogen Bonding, Isomerism, Molecular Conformation, Peptides, Rotaxanes
Abstract

<p>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.</p>

DOI10.1002/chem.202103615
Alternate JournalChemistry
PubMed ID34797593
PubMed Central IDPMC8792204
Grant ListGM128813 / GM / NIGMS NIH HHS / United States
R35 GM128813 / GM / NIGMS NIH HHS / United States
R01 GM107036 / GM / NIGMS NIH HHS / United States
427725459 / / Deutsche Forschungsgemeinschaft /
GM107036 / GM / NIGMS NIH HHS / United States