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Enzyme-Degradable Self-Assembled Nanostructures from Polymer-Peptide Hybrids

dc.rights.licenseopen
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierInstitute for Nanotechnology [Waterloo]
dc.contributor.authorBACINELLO, Daniel
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierImagerie Moléculaire et Nanobiotechnologies - Institut Européen de Chimie et Biologie [IECB]
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 1 LCPO : Polymerization Catalyses & Engineering
dc.contributor.authorTATON, Daniel
hal.structure.identifierInstitute for Nanotechnology [Waterloo]
dc.contributor.authorTAM, Kam Chiu
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.issued2014
dc.identifier.issn1525-7797
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/20209
dc.description.abstractEnThe peptide PVGLIG, which is known to be selectively cleaved by the tumor-associated enzyme matrix metalloproteinase-2 (MMP-2), was conjugated to a-alkene poly(trimethylene carbonate) (PTMC) blocks of varying sizes via UV-initiated thiol-ene "click" chemistry. The PTMC precursor was synthesized by metal-free ring-opening polymerization using ally! alcohol as an initiator and an N-heterocyclic carbene as an organic catalyst. The unprecedented PVGLIG-b-PTMC hybrids were self-assembled in aqueous solution and various submicrometer-sized morphologies obtained by a nanoprecipitation process. Characterization of particle morphology was carried out by multiangle dynamic light scattering (DLS) and static light scattering (SLS) evidencing spherical nanoparticles with different morphologies and narrow size distributions. Microstructure details were also observed on transmission electron micrographs and were in good agreement with light scattering measurements showing the assembly of core shell, large compound micelles, and vesicle morphologies, the particle morphology varying with the hydrophilic weight fractions (f) of the hybrids. These nanostructures displayed selective degradation in the presence of the cancer-associated enzyme MMP-2, as probed by the morphological change both by TEM and DLS. All these results demonstrated that PVGLIG-b-PTMC hybrids were suitable to target the tumor microenvironment.
dc.language.isoen
dc.publisherAmerican Chemical Society
dc.subject.enRING-OPENING POLYMERIZATION
dc.subject.enBLOCK-COPOLYMERS
dc.subject.enDRUG-DELIVERY
dc.subject.enMICELLES
dc.subject.enNANOPARTICLES
dc.subject.enCHIMERAS
dc.subject.enCARRIERS
dc.title.enEnzyme-Degradable Self-Assembled Nanostructures from Polymer-Peptide Hybrids
dc.typeArticle de revue
dc.identifier.doi10.1021/bm500296n
dc.subject.halChimie/Polymères
bordeaux.journalBiomacromolecules
bordeaux.page1882-1888
bordeaux.volume15
bordeaux.hal.laboratoriesLaboratoire de Chimie des Polymères Organiques (LCPO) - UMR 5629*
bordeaux.issue5
bordeaux.institutionBordeaux INP
bordeaux.institutionUniversité de Bordeaux
bordeaux.peerReviewedoui
hal.identifierhal-01369962
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-01369962v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Biomacromolecules&rft.date=2014&rft.volume=15&rft.issue=5&rft.spage=1882-1888&rft.epage=1882-1888&rft.eissn=1525-7797&rft.issn=1525-7797&rft.au=BACINELLO,%20Daniel&GARANGER,%20Elisabeth&TATON,%20Daniel&TAM,%20Kam%20Chiu&LECOMMANDOUX,%20Sebastien&rft.genre=article


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