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Article: Dynamic force spectroscopy of synthetic oligorotaxane foldamers

TitleDynamic force spectroscopy of synthetic oligorotaxane foldamers
Authors
KeywordsAFM
Equilibrium dynamics
Foldamers
Molecular machines
Single-molecule force spectroscopy
Issue Date2018
Citation
Proceedings of the National Academy of Sciences of the United States of America, 2018, v. 115, n. 38, p. 9362-9366 How to Cite?
AbstractWholly synthetic molecules involving both mechanical bonds and a folded secondary structure are one of the most promising architectures for the design of functional molecular machines with unprecedented properties. Here, we report dynamic single-molecule force spectroscopy experiments that explore the energetic details of donor–acceptor oligorotaxane foldamers, a class of molecular switches. The mechanical breaking of the donor–acceptor interactions responsible for the folded structure shows a high constant rupture force over a broad range of loading rates, covering three orders of magnitude. In comparison with dynamic force spectroscopy performed during the past 20 y on various (bio)molecules, the near-equilibrium regime of oligorotaxanes persists at much higher loading rates, at which biomolecules have reached their kinetic regime, illustrating the very fast dynamics and remarkable rebinding capabilities of the intramolecular donor–acceptor interactions. We focused on one single interaction at a time and probed the stochastic rupture and rebinding paths. Using the Crooks fluctuation theorem, we measured the mechanical work produced during the breaking and rebinding to determine a free-energy difference, ΔG, of 6 kcal·mol−1 between the two local conformations around a single bond.
Persistent Identifierhttp://hdl.handle.net/10722/333694
ISSN
2023 Impact Factor: 9.4
2023 SCImago Journal Rankings: 3.737
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorSluysmans, Damien-
dc.contributor.authorDevaux, Floriane-
dc.contributor.authorBruns, Carson J.-
dc.contributor.authorFraser Stoddart, J.-
dc.contributor.authorDuwez, Anne Sophie-
dc.date.accessioned2023-10-06T05:21:39Z-
dc.date.available2023-10-06T05:21:39Z-
dc.date.issued2018-
dc.identifier.citationProceedings of the National Academy of Sciences of the United States of America, 2018, v. 115, n. 38, p. 9362-9366-
dc.identifier.issn0027-8424-
dc.identifier.urihttp://hdl.handle.net/10722/333694-
dc.description.abstractWholly synthetic molecules involving both mechanical bonds and a folded secondary structure are one of the most promising architectures for the design of functional molecular machines with unprecedented properties. Here, we report dynamic single-molecule force spectroscopy experiments that explore the energetic details of donor–acceptor oligorotaxane foldamers, a class of molecular switches. The mechanical breaking of the donor–acceptor interactions responsible for the folded structure shows a high constant rupture force over a broad range of loading rates, covering three orders of magnitude. In comparison with dynamic force spectroscopy performed during the past 20 y on various (bio)molecules, the near-equilibrium regime of oligorotaxanes persists at much higher loading rates, at which biomolecules have reached their kinetic regime, illustrating the very fast dynamics and remarkable rebinding capabilities of the intramolecular donor–acceptor interactions. We focused on one single interaction at a time and probed the stochastic rupture and rebinding paths. Using the Crooks fluctuation theorem, we measured the mechanical work produced during the breaking and rebinding to determine a free-energy difference, ΔG, of 6 kcal·mol−1 between the two local conformations around a single bond.-
dc.languageeng-
dc.relation.ispartofProceedings of the National Academy of Sciences of the United States of America-
dc.subjectAFM-
dc.subjectEquilibrium dynamics-
dc.subjectFoldamers-
dc.subjectMolecular machines-
dc.subjectSingle-molecule force spectroscopy-
dc.titleDynamic force spectroscopy of synthetic oligorotaxane foldamers-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1073/pnas.1712790115-
dc.identifier.pmid29279384-
dc.identifier.scopuseid_2-s2.0-85053525652-
dc.identifier.volume115-
dc.identifier.issue38-
dc.identifier.spage9362-
dc.identifier.epage9366-
dc.identifier.eissn1091-6490-
dc.identifier.isiWOS:000447224900033-

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