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Single-molecule mechanical unfolding experiments reveal a critical length for the formation of α-helices in peptides

dc.rights.licenseopen
hal.structure.identifierMolecular Systems Research Unit, University of Liège
dc.contributor.authorSLUYSMANS, Damien
hal.structure.identifierMolecular Systems Research Unit, University of Liège
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
dc.contributor.authorWILLET, Nicolas
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
dc.contributor.authorTHEVENOT, Julie
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
dc.contributor.authorLECOMMANDOUX, Sebastien
hal.structure.identifierMolecular Systems Research Unit, University of Liège
dc.contributor.authorDUWEZ, Anne-Sophie
dc.date.accessioned2020
dc.date.available2020
dc.date.issued2020
dc.identifier.issn2055-6756
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/19699
dc.description.abstractEnα-Helix is the most predominant secondary structure in proteins and supports many functions in biological machineries. The conformation of the helix is dictated by many factors such as its primary sequence, intramolecular interactions, or the effect of the close environment. Several computational studies have proposed that there is a critical maximum length for the formation of intact compact helical structures, supporting the fact that most intact α-helices in proteins are constituted of a small number of amino acids. To obtain a detailed picture on the formation of α-helices in peptides and their mechanical stability, we have synthesized a long homopolypeptide of about 90 amino acids, poly(γ-benzyl-L-glutamate), and investigated its mechanical behaviour by AFM-based single-molecule force spectroscopy. The characteristic plateaus observed in the force–extension curves reveal the unfolding of a series of small helices (from 1 to 4) of about 20 amino acid residues connected to each other, rather than a long helix of 90 residues. Our results suggest the formation of a tertiary structure made of short helices with kinks, instead of an intact compact helical structure for sequences of more than 20 amino acid residues. To our knowledge, this is the first experimental evidence supporting the concept of a helical critical length previously proposed by several computational studies.
dc.language.isoen
dc.publisherRoyal Society of Chemistry
dc.title.enSingle-molecule mechanical unfolding experiments reveal a critical length for the formation of α-helices in peptides
dc.typeArticle de revue
dc.identifier.doi10.1039/D0NH00036A
dc.subject.halChimie/Polymères
dc.subject.halPhysique [physics]/Matière Condensée [cond-mat]/Matière Molle [cond-mat.soft]
dc.subject.halSciences du Vivant [q-bio]/Ingénierie biomédicale/Biomatériaux
bordeaux.journalNanoscale Horizons
bordeaux.page671-678
bordeaux.volume5
bordeaux.hal.laboratoriesLaboratoire de Chimie des Polymères Organiques (LCPO) - UMR 5629*
bordeaux.issue4
bordeaux.institutionBordeaux INP
bordeaux.institutionUniversité de Bordeaux
bordeaux.peerReviewedoui
hal.identifierhal-02507311
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02507311v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Nanoscale%20Horizons&rft.date=2020&rft.volume=5&rft.issue=4&rft.spage=671-678&rft.epage=671-678&rft.eissn=2055-6756&rft.issn=2055-6756&rft.au=SLUYSMANS,%20Damien&WILLET,%20Nicolas&THEVENOT,%20Julie&LECOMMANDOUX,%20Sebastien&DUWEZ,%20Anne-Sophie&rft.genre=article


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