Site-directed conjugation of "Clicked" glycopolymers to form glycoprotein mimics: Binding to mammalian lectin and induction of immunological function Geng, J. en_US Mantovani, G. en_US Tao, L. en_US Nicolas, J. en_US Chen, Gaojian en_US Wallis, R. en_US Mitchell, D. A. en_US Johnson, B. R. G. en_US Evans, S. D. en_US Haddleton, D. M. en_US 2021-11-25T14:08:46Z 2021-11-25T14:08:46Z 2007 en_US
dc.description.abstract Synthesis of well-defined neoglycopolymer-protein biohybrid materials and a preliminary study focused on their ability of binding mammalian lectins and inducing immunological function is reported. Crucial intermediates for their preparation are well-defined maleimide-terminated neoglycopolymers (M-n = 8-30 kDa; M-w/M-n = 1.20-1.28) presenting multiple copies of mannose epitope units, obtained by combination of transition-metal-mediated living radical polymerization (TMM LRP) and Huisgen [2+3] cycloaddition. Bovine serum albumin (BSA) was employed as single thiol-containing model protein, and the resulting bioconjugates were purified following two independent protocols and characterized by circular dichroism (CD) spectroscopy, SDS PAGE, and SEC HPLC. The versatility of the synthetic strategy presented in this work was demonstrated by preparing a small library of conjugating glycopolymers that only differ from each other for their relative epitope density were prepared by coclicking of appropriate mixtures of mannopyranoside and galactopyranoside azides to the same polyalkyne scaffold intermediate. Surface plasmon resonance binding studies carried out using recombinant rat mannose-binding lectin (MBL) showed clear and dose-dependent MBL binding to glycopolymer-conjugated BSA. In addition, enzyme-linked immunosorbent assay (ELISA) revealed that the neoglycopolymer-protein materials described in this work possess significantly enhanced capacity to activate complement via the lectin pathway when compared with native unmodified BSA. en_US
dc.language English
dc.language.iso EN en_US
dc.rights CC BY-NC-ND 3.0 en_US
dc.rights.uri en_US
dc.source Legacy MARC en_US
dc.title Site-directed conjugation of "Clicked" glycopolymers to form glycoprotein mimics: Binding to mammalian lectin and induction of immunological function en_US
dc.type Journal Article en
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dspace.entity.type Publication en_US
unsw.identifier.doiPublisher en_US
unsw.relation.faculty Engineering
unsw.relation.ispartofissue 49 en_US
unsw.relation.ispartofjournal Journal of the American Chemical Society en_US
unsw.relation.ispartofpagefrompageto 15156-15163 en_US
unsw.relation.ispartofvolume 129 en_US
unsw.relation.originalPublicationAffiliation Geng, J. en_US
unsw.relation.originalPublicationAffiliation Mantovani, G. en_US
unsw.relation.originalPublicationAffiliation Tao, L. en_US
unsw.relation.originalPublicationAffiliation Nicolas, J. en_US
unsw.relation.originalPublicationAffiliation Chen, Gaojian, Chemical Sciences & Engineering, Faculty of Engineering, UNSW en_US
unsw.relation.originalPublicationAffiliation Wallis, R. en_US
unsw.relation.originalPublicationAffiliation Mitchell, D. A. en_US
unsw.relation.originalPublicationAffiliation Johnson, B. R. G. en_US
unsw.relation.originalPublicationAffiliation Evans, S. D. en_US
unsw.relation.originalPublicationAffiliation Haddleton, D. M. en_US School of Chemical Engineering *
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