Title | The Shuttling Cascade in Lasso Peptide Benenodin-1 is Controlled by Non-Covalent Interactions. |
Publication Type | Journal Article |
Year of Publication | 2022 |
Authors | Schröder, HV, Stadlmeier, M, Wühr, M, A Link, J |
Journal | Chemistry |
Volume | 28 |
Issue | 5 |
Pagination | e202103615 |
Date Published | 2022 Jan 24 |
ISSN | 1521-3765 |
Keywords | Hydrogen 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> |
DOI | 10.1002/chem.202103615 |
Alternate Journal | Chemistry |
PubMed ID | 34797593 |
PubMed Central ID | PMC8792204 |
Grant List | GM128813 / GM / NIGMS NIH HHS / United States R35 GM128813 / GM / NIGMS NIH HHS / United States R01 GM107036 / GM / NIGMS NIH HHS / United States GM107036 / GM / NIGMS NIH HHS / United States |