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dc.rights.licenseopen
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
dc.contributor.authorGAUCHE, Cony
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.issued2016
dc.identifier.issn0032-3861
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/20150
dc.description.abstractEnThe understanding of glycopolymer-based nanostructures formation and their lectin binding properties are of great interest to the development of drug delivery systems and other biological applications. Herein, glycosylated polypeptides were synthesized from a clickable poly(L-lysine)-b-poly(benzyl-L-glutamate) copolypeptide, obtained by a sequential ring opening polymerization. The clickable poly(L-lysine) chain was completely functionalized by introducing galactose and lactose moieties on the copolypeptide's hydrophilic block, aiming specific lectin recognition. Spheres, pearl-necklace and worm-like structures prepared from poly(L-lysine)-b-poly(benzyl-L-glutamate) copolypeptides were obtained after nanoprecipitation, depending on the hydrophilic block functionalization and the hydrophobic block length. Specific interaction between the sugars on the micelles' surface with RCA120 lectin was observed with the PBLG40-based nano-structures. However, unexpected and unspecific interactions were observed with some nanostructures, showing the importance of the chemical functionalization and nanostructure stabilization. Such a synthetic approach can be used to develop any other amphiphilic and biofunctional polypeptide-based copolymers and nanoparticles.
dc.language.isoen
dc.publisherElsevier
dc.subject.enCopolymer
dc.subject.enSelf-assembly
dc.subject.enMicelles
dc.title.enVersatile design of amphiphilic glycopolypeptides nanoparticles for lectin recognition
dc.typeArticle de revue
dc.identifier.doi10.1016/j.polymer.2016.08.077
dc.subject.halChimie/Polymères
bordeaux.journalPolymer
bordeaux.page474-484
bordeaux.volume107
bordeaux.hal.laboratoriesLaboratoire de Chimie des Polymères Organiques (LCPO) - UMR 5629*
bordeaux.institutionBordeaux INP
bordeaux.institutionUniversité de Bordeaux
bordeaux.peerReviewedoui
hal.identifierhal-01417441
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-01417441v1
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