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Dynamic Spatial Formation and Distribution of Intrinsically Disordered Protein Droplets in Macromolecularly Crowded Protocells

dc.rights.licenseopen
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
dc.contributor.authorZHAO, Hang
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
dc.contributor.authorIBRAHIMOVA, Vusala
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.authorLECOMMANDOUX, Sebastien
dc.date.accessioned2020
dc.date.available2020
dc.date.issued2020
dc.identifier.issn1433-7851
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/19698
dc.description.abstractEnElastin‐like polypeptides (ELPs) have been proposed as a simple model of intrinsically disordered proteins (IDPs) which can form membrane‐less organelles via liquid‐liquid phase separation (LLPS) in cellular milieu. Herein, fluorescently labeled ELP is studied in cytomimetic aqueous two‐phase system (ATPS). Droplet‐based protocells are obtained in a microfluidic system, allowing for confinement, temperature changes and statistical analysis. The spatial organization of ELP is observed in such binary ATPS macrocrowders. In addition, owing to switch of conformational states, dynamic formation and distribution of ELP‐rich droplets within the artificial cytoplasm is triggered by temperature. Three‐dimensional structured proteins are concurrently encapsulated along with ELP in synthetic cells and distinct partitioning properties of these proteins and ELP in binary polymeric phases are observed. This underpinning discovery demonstrates that the ability of ELP to coacervate with temperature can be maintained inside intracellular mimetic medium, and the preferential distribution of ELP in macromolecular crowding.
dc.description.sponsorshipIdEx Bordeaux - ANR-10-IDEX-0003-02/10-IDEX-0003
dc.language.isoen
dc.publisherWiley-VCH Verlag
dc.subject.enIntrinsically disordered proteins (IDP)
dc.subject.enElastin‐like polypeptides (ELP)
dc.subject.ensynthetic cell
dc.subject.enminimal cell
dc.subject.enmacromolecular crowding
dc.subject.enaqueous two‐phase system (ATPS)
dc.title.enDynamic Spatial Formation and Distribution of Intrinsically Disordered Protein Droplets in Macromolecularly Crowded Protocells
dc.typeArticle de revue
dc.identifier.doi10.1002/anie.202001868
dc.subject.halPhysique [physics]/Matière Condensée [cond-mat]/Matière Molle [cond-mat.soft]
dc.subject.halChimie/Polymères
dc.subject.halSciences du Vivant [q-bio]/Biotechnologies
dc.description.sponsorshipEuropeTemperature-responsive polypeptide nanocarriers for abdominal therapies
bordeaux.journalAngewandte Chemie International Edition
bordeaux.page11028-11036
bordeaux.volume59
bordeaux.hal.laboratoriesLaboratoire de Chimie des Polymères Organiques (LCPO) - UMR 5629*
bordeaux.issue27
bordeaux.institutionBordeaux INP
bordeaux.institutionUniversité de Bordeaux
bordeaux.peerReviewedoui
hal.identifierhal-02519909
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02519909v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Angewandte%20Chemie%20International%20Edition&rft.date=2020&rft.volume=59&rft.issue=27&rft.spage=11028-11036&rft.epage=11028-11036&rft.eissn=1433-7851&rft.issn=1433-7851&rft.au=ZHAO,%20Hang&IBRAHIMOVA,%20Vusala&GARANGER,%20Elisabeth&LECOMMANDOUX,%20Sebastien&rft.genre=article


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