Tailored drug-release from multi-functional polymer-peptide hybrid vesicles
dc.rights.license | open | |
hal.structure.identifier | Laboratoire de Chimie des Polymères Organiques [LCPO] | |
hal.structure.identifier | Institute for Nanotechnology [Waterloo] | |
hal.structure.identifier | Team 3 LCPO : Polymer Self-Assembly & Life Sciences | |
dc.contributor.author | BACINELLO, Daniel | |
hal.structure.identifier | Laboratoire de Chimie des Polymères Organiques [LCPO] | |
hal.structure.identifier | Institut Européen de Chimie et Biologie [IECB] | |
hal.structure.identifier | Team 3 LCPO : Polymer Self-Assembly & Life Sciences | |
dc.contributor.author | GARANGER, Elisabeth
IDREF: 089451740 | |
hal.structure.identifier | Laboratoire de Chimie des Polymères Organiques [LCPO] | |
hal.structure.identifier | Team 1 LCPO : Polymerization Catalyses & Engineering | |
dc.contributor.author | TATON, Daniel | |
hal.structure.identifier | Institute for Nanotechnology [Waterloo] | |
dc.contributor.author | TAM, Kam Chiu | |
hal.structure.identifier | Laboratoire de Chimie des Polymères Organiques [LCPO] | |
hal.structure.identifier | Team 3 LCPO : Polymer Self-Assembly & Life Sciences | |
dc.contributor.author | LECOMMANDOUX, Sebastien | |
dc.date.accessioned | 2020 | |
dc.date.available | 2020 | |
dc.date.issued | 2015 | |
dc.identifier.issn | 0014-3057 | |
dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/20265 | |
dc.description.abstractEn | The 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.iso | en | |
dc.publisher | Elsevier | |
dc.subject.en | BLOCK-COPOLYMERS | |
dc.subject.en | Polymersome | |
dc.subject.en | NANOCARRIERS | |
dc.subject.en | DELIVERY | |
dc.subject.en | MICELLES | |
dc.subject.en | Matrix metalloproteinase | |
dc.subject.en | Drug delivery systems | |
dc.subject.en | Poly(trimethylene carbonate) | |
dc.subject.en | Thiol-ene | |
dc.subject.en | Cancer targeting | |
dc.title.en | Tailored drug-release from multi-functional polymer-peptide hybrid vesicles | |
dc.type | Article de revue | |
dc.identifier.doi | 10.1016/j.eurpolymj.2014.09.001 | |
dc.subject.hal | Chimie/Polymères | |
bordeaux.journal | European Polymer Journal | |
bordeaux.page | 363-373 | |
bordeaux.volume | 62 | |
bordeaux.hal.laboratories | Laboratoire de Chimie des Polymères Organiques (LCPO) - UMR 5629 | * |
bordeaux.institution | Bordeaux INP | |
bordeaux.institution | Université de Bordeaux | |
bordeaux.peerReviewed | oui | |
hal.identifier | hal-01361862 | |
hal.version | 1 | |
hal.origin.link | https://hal.archives-ouvertes.fr//hal-01361862v1 | |
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