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dc.rights.licenseopenen_US
hal.structure.identifierInstitut des Sciences Moléculaires [ISM]
dc.contributor.authorGRAZON, Chloé
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
dc.contributor.authorGARANGER, Elisabeth
IDREF: 089451740
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
dc.contributor.authorLALANNE, Pierre
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
dc.contributor.authorIBARBOURE, Emmanuel
hal.structure.identifierBoston University [Boston] [BU]
dc.contributor.authorGALAGAN, James E
hal.structure.identifierDepartment of Chemistry and Chemical Biology [Boston]
dc.contributor.authorGRINSTAFF, Mark W
dc.date.accessioned2023-10-29T15:49:14Z
dc.date.available2023-10-29T15:49:14Z
dc.date.issued2023-10-25
dc.identifier.issn1526-4602en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/184554
dc.description.abstractEnPolymeric micelles and especially those based on natural diblocks are of particular interest due to their advantageous properties in terms of molecular recognition, biocompatibility, and biodegradability. We herein report a facile and straightforward synthesis of thermoresponsive elastin-like polypeptide (ELP) and oligonucleotide (ON) diblock bioconjugates, ON--ELP, through copper-catalyzed azide-alkyne cycloaddition. The resulting thermosensitive diblock copolymer self-assembles above its critical micelle temperature (CMT ∼30 °C) to form colloidally stable micelles of ∼50 nm diameter. The ON--ELP micelles hybridize with an ON complementary strand and maintain their size and stability. Next, we describe the capacity of these micelles to bind proteins, creating more complex structures using the classic biotin-streptavidin pairing and the specific recognition between a transcription factor protein and the ON strand. In both instances, the micelles are intact, form larger structures, and retain their sensitivity to temperature.
dc.language.isoENen_US
dc.rightsAttribution-NonCommercial-ShareAlike 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/us/*
dc.subject.enChemical biology
dc.subject.enHydrodynamics
dc.subject.enMicelles
dc.subject.enOrganic compounds
dc.title.enTranscription-Factor-Induced Aggregation of Biomimetic Oligonucleotide--Protein Micelles.
dc.title.alternativeBiomacromoleculesen_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1021/acs.biomac.3c00662en_US
dc.subject.halChimie/Polymèresen_US
dc.subject.halSciences du Vivant [q-bio]/Biotechnologiesen_US
dc.identifier.pubmed37877162en_US
bordeaux.journalBiomacromoleculesen_US
bordeaux.pageDOI: 10.1021/acs.biomac.3c00662en_US
bordeaux.volume24en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcepubmed
hal.identifierhal-04263919
hal.version1
hal.date.transferred2023-10-29T15:49:17Z
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exporttrue
workflow.import.sourcepubmed
dc.rights.ccCC BY-NC-SAen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Biomacromolecules&rft.date=2023-10-25&rft.volume=24&rft.spage=DOI:%2010.1021/acs.biomac.3c00662&rft.epage=DOI:%2010.1021/acs.biomac.3c00662&rft.eissn=1526-4602&rft.issn=1526-4602&rft.au=GRAZON,%20Chlo%C3%A9&GARANGER,%20Elisabeth&LALANNE,%20Pierre&IBARBOURE,%20Emmanuel&GALAGAN,%20James%20E&rft.genre=article


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