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Adaptive Binding of Alkyl Glycosides by Nonpeptidic Helix Bundles in Water: Toward Artificial Glycolipid Binding Proteins

dc.rights.licenseopenen_US
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorYOO, Sung Hyun
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorBURATTO, Jeremie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorROY, Arup
dc.contributor.authorMORVAN, Estelle
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorPASCO, Morgane
dc.contributor.authorPULKA-ZIACH, Karolina
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLOMBARDO, Caterina M.
dc.contributor.authorROSU, Frederic
dc.contributor.authorGABELICA, Valerie
dc.contributor.authorMACKERETH, Cameron D.
dc.contributor.authorCOLLIE, Gavin W.
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorGUICHARD, Gilles
dc.date.accessioned2023-04-18T13:21:52Z
dc.date.available2023-04-18T13:21:52Z
dc.date.issued2022-08-23
dc.identifier.issn0002-7863en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/173076
dc.description.abstractEnAmphipathic water-soluble helices formed from synthetic peptides or foldamers are promising building blocks for the creation of self-assembled architectures with non-natural shapes and functions. While rationally designed artificial quaternary structures such as helix bundles have been shown to contain preformed cavities suitable for guest binding, there are no examples of adaptive binding of guest molecules by such assemblies in aqueous conditions. We have previously reported a foldamer 6-helix bundle that contains an internal nonpolar cavity able to bind primary alcohols as guest molecules. Here, we show that this 6-helix bundle can also interact with larger, more complex guests such as n-alkyl glycosides. X-ray diffraction analysis of co-crystals using a diverse set of guests together with solution and gas-phase studies reveals an adaptive binding mode whereby the apo form of the 6-helix bundle undergoes substantial conformational change to accommodate the hydrocarbon chain in a manner reminiscent of glycolipid transfer proteins in which the cavity forms upon lipid uptake. The dynamic nature of the self-assembling and molecular recognition processes reported here marks a step forward in the design of functional proteomimetic molecular assemblies.
dc.description.sponsorshipMimétisme et ingénierie d'enzymes artificielles à l'aide de foldamères - ANR-17-CE07-0020en_US
dc.language.isoENen_US
dc.title.enAdaptive Binding of Alkyl Glycosides by Nonpeptidic Helix Bundles in Water: Toward Artificial Glycolipid Binding Proteins
dc.title.alternativeJ. Am. Chem. Soc.en_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1021/jacs.2c05234en_US
dc.subject.halChimie/Matériauxen_US
dc.description.sponsorshipEuropeBioinspired Nanostructures by Self-assembly of Amphiphilic Non-peptide Helical Foldamers in Aqueous Environmenten_US
bordeaux.journalJournal of the American Chemical Societyen_US
bordeaux.page15988-15998en_US
bordeaux.volume144en_US
bordeaux.hal.laboratoriesCBMN : Chimie & de Biologie des Membranes & des Nano-objets - UMR 5248en_US
bordeaux.issue35en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.exportfalse
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Journal%20of%20the%20American%20Chemical%20Society&rft.date=2022-08-23&rft.volume=144&rft.issue=35&rft.spage=15988-15998&rft.epage=15988-15998&rft.eissn=0002-7863&rft.issn=0002-7863&rft.au=YOO,%20Sung%20Hyun&BURATTO,%20Jeremie&ROY,%20Arup&MORVAN,%20Estelle&PASCO,%20Morgane&rft.genre=article


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