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hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierInstitute for Nanotechnology [Waterloo]
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
dc.contributor.authorBACINELLO, Daniel
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierInstitut 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.issued2015
dc.identifier.issn0014-3057
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/20265
dc.description.abstractEnThe synthetic semi-crystalline polymer poly(trimethylene carbonate) PTMC50 was linked to the synthetic poly(amino acid) poly(glutamic acid) (PGA(15)) using the peptide PVGLIG, known to be selectively cleaved by the tumor-associated enzyme matrix metalloproteinase 2 (MMP-2), by a combination of thiol-ene coupling and ring-opening polymerization. Stable, monodisperse, sub-micron sized polymersomes were subsequently obtained by self-assembly and characterized by dynamic and static light scattering (DLS and SLS) and transmission electron microscopy (TEM). These vesicles showed selective degradation in the presence of MMP-2 as probed by DLS. The model drug imipramine hydrochloride was loaded at 35% encapsulation efficiency by co-precipitation and displayed controlled drug-release behavior. Drug release rates showed several fold increases when exposed to pH, temperature and most significantly, to the tumor-associated enzyme MMP-2. Such structures, bearing precise location of the cleavable peptide sequence, may hold promise as future specific and controlled drug-delivery systems. (C) 2014 Elsevier Ltd. All rights reserved.
dc.language.isoen
dc.publisherElsevier
dc.subject.enBLOCK-COPOLYMERS
dc.subject.enPolymersome
dc.subject.enNANOCARRIERS
dc.subject.enDELIVERY
dc.subject.enMICELLES
dc.subject.enMatrix metalloproteinase
dc.subject.enDrug delivery systems
dc.subject.enPoly(trimethylene carbonate)
dc.subject.enThiol-ene
dc.subject.enCancer targeting
dc.title.enTailored drug-release from multi-functional polymer-peptide hybrid vesicles
dc.typeArticle de revue
dc.identifier.doi10.1016/j.eurpolymj.2014.09.001
dc.subject.halChimie/Polymères
bordeaux.journalEuropean Polymer Journal
bordeaux.page363-373
bordeaux.volume62
bordeaux.hal.laboratoriesLaboratoire de Chimie des Polymères Organiques (LCPO) - UMR 5629*
bordeaux.institutionBordeaux INP
bordeaux.institutionUniversité de Bordeaux
bordeaux.peerReviewedoui
hal.identifierhal-01361862
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-01361862v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=European%20Polymer%20Journal&rft.date=2015&rft.volume=62&rft.spage=363-373&rft.epage=363-373&rft.eissn=0014-3057&rft.issn=0014-3057&rft.au=BACINELLO,%20Daniel&GARANGER,%20Elisabeth&TATON,%20Daniel&TAM,%20Kam%20Chiu&LECOMMANDOUX,%20Sebastien&rft.genre=article


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