Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-705
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dc.contributor.authorBeck, Simone-
dc.contributor.authorSchultze, Jennifer-
dc.contributor.authorRäder, Hans-Joachim-
dc.contributor.authorHolm, Regina-
dc.contributor.authorSchinnerer, Meike-
dc.contributor.authorBarz, Matthias-
dc.contributor.authorKoynov, Kaloian-
dc.contributor.authorZentel, Rudolf-
dc.date.accessioned2019-01-23T10:52:31Z-
dc.date.available2019-01-23T11:52:31Z-
dc.date.issued2018-
dc.identifier.urihttps://openscience.ub.uni-mainz.de/handle/20.500.12030/707-
dc.description.abstractThe design of multifunctional polymer-based vectors, forming pDNA vaccines, offers great potential in cancer immune therapy. The transfection of dendritic immune cells (DCs) with tumour antigen-encoding pDNA leads to an activation of the immune system to combat tumour cells. In this work, we investigated the chemical attachment of DEC205 antibodies (aDEC205) as DC-targeting structures to polyplexes of P(Lys)-b-P(HPMA). The conjugation of a synthetic block copolymer and a biomacromolecule with various functionalities (aDEC205) requires bioorthogonal techniques to avoid side reactions. Click chemistry and in particular the strain-promoted alkyne-azide cycloaddition (SPAAC) can provide the required bioorthogonality. With regard to a SPAAC of both components, we firstly synthesized two different azide-containing block copolymers, P(Lys)-b-P(HPMA)-N3(stat) and P(Lys)-b-P(HPMA)-N3(end), for pDNA complexation. In addition, the site-specific incorporation of ring-strained dibenzocyclooctyne (DBCO) moieties to the DEC205 antibody was achieved by an enzymatic strategy using bacterial transglutaminase (BTG). The chemical accessibility of DBCO molecules within aDEC205 as well as the accessibility of azide-functionalities on the polyplex’ surface were investigated by various SPAAC experiments and characterized by fluorescence correlation spectroscopy (FCS).en_GB
dc.description.sponsorshipDFG, Open Access-Publizieren Universität Mainz / Universitätsmedizin-
dc.language.isoeng-
dc.rightsCC BYde_DE
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/-
dc.subject.ddc540 Chemiede_DE
dc.subject.ddc540 Chemistry and allied sciencesen_GB
dc.titleSite-specific DBCO modification of DEC205 antibody for polymer conjugationen_GB
dc.typeZeitschriftenaufsatzde_DE
dc.identifier.urnurn:nbn:de:hebis:77-publ-588003-
dc.identifier.doihttp://doi.org/10.25358/openscience-705-
jgu.type.dinitypearticle-
jgu.type.versionPublished versionen_GB
jgu.type.resourceText-
jgu.organisation.departmentFB 09 Chemie, Pharmazie u. Geowissensch.-
jgu.organisation.number7950-
jgu.organisation.nameJohannes Gutenberg-Universität Mainz-
jgu.rights.accessrightsopenAccess-
jgu.journal.titlePolymers-
jgu.journal.volume10-
jgu.journal.issue2-
jgu.pages.alternativeArt. 141-
jgu.publisher.year2018-
jgu.publisher.nameMDPI-
jgu.publisher.placeBasel-
jgu.publisher.urihttp://dx.doi.org/10.3390/polym10020141-
jgu.publisher.issn2073-4360-
jgu.organisation.placeMainz-
jgu.subject.ddccode540-
opus.date.accessioned2019-01-23T10:52:31Z-
opus.date.modified2019-01-23T11:03:22Z-
opus.date.available2019-01-23T11:52:31-
opus.subject.dfgcode00-000-
opus.organisation.stringFB 09: Chemie, Pharmazie und Geowissenschaften: Institut für Organische Chemiede_DE
opus.identifier.opusid58800-
opus.institute.number0905-
opus.metadataonlyfalse-
opus.type.contenttypeKeinede_DE
opus.type.contenttypeNoneen_GB
opus.affiliatedBarz, Matthias-
opus.affiliatedZentel, Rudolf-
jgu.publisher.doi10.3390/polym10020141
jgu.organisation.rorhttps://ror.org/023b0x485
Appears in collections:JGU-Publikationen

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