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dc.rights.licenseopenen_US
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorYOO, Sung Hyun
hal.structure.identifierInstitut Européen de Chimie et Biologie [IECB]
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLI, Bo
hal.structure.identifierInstitut Européen de Chimie et Biologie [IECB]
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorDOLAIN, Christel
hal.structure.identifierInstitut Européen de Chimie et Biologie [IECB]
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorPASCO, Morgane
IDREF: 152520791
hal.structure.identifierInstitut Européen de Chimie et Biologie [IECB]
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorGUICHARD, Gilles
IDREF: 084339268
dc.date.accessioned2021-11-15T07:26:34Z
dc.date.available2021-11-15T07:26:34Z
dc.date.issued2021-06-04
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/123793
dc.description.abstractEnN,N'-linked oligoureas are a class of enantiopure, sequence-defined peptidomimetic oligomers without amino acids that form well-defined and predictable helical structures akin to the peptide α-helix. Oligourea-based foldamers combine a number of features-such as synthetic accessibility, sequence modularity, and folding fidelity-that bode well for their use in a range of applications from medicinal chemistry to catalysis. Moreover, it was recently recognized that this synthetic helical backbone can be combined with regular peptides to generate helically folded peptide-oligourea hybrids that display additional features in terms of helix mimicry and protein-surface recognition properties. Here we provide detailed protocols for the preparation of requested monomers and for the synthesis and purification of homo-oligoureas and peptide-oligourea hybrids.
dc.description.sponsorshipHélices chimériques aux propriétés innovantes pour l'inhibition des interactions protéine-protéine - ANR-15-CE07-0010en_US
dc.description.sponsorshipMimétisme et ingénierie d'enzymes artificielles à l'aide de foldamères - ANR-17-CE07-0020en_US
dc.language.isoENen_US
dc.source.titleMethods in Enzymology Volume 656en_US
dc.subject.enModels
dc.subject.enMolecular
dc.subject.enPeptides
dc.subject.enPeptidomimetics
dc.subject.enProtein Conformation
dc.subject.enalpha-Helical
dc.subject.enUrea
dc.title.enUrea based foldamers
dc.title.alternativeMethods Enzymolen_US
dc.typeChapitre d'ouvrageen_US
dc.identifier.doi10.1016/bs.mie.2021.04.019en_US
dc.subject.halChimieen_US
dc.identifier.pubmed34325800en_US
bordeaux.page59-92en_US
bordeaux.volume656en_US
bordeaux.hal.laboratoriesUMR 5248en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.inpressnonen_US
bordeaux.import.sourcepubmed
hal.identifierhal-03428128
hal.version1
hal.date.transferred2021-11-15T07:26:41Z
hal.exporttrue
workflow.import.sourcepubmed
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.btitle=Methods%20in%20Enzymology%20Volume%20656&rft.date=2021-06-04&rft.volume=656&rft.spage=59-92&rft.epage=59-92&rft.au=YOO,%20Sung%20Hyun&LI,%20Bo&DOLAIN,%20Christel&PASCO,%20Morgane&GUICHARD,%20Gilles&rft.genre=unknown


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