[J. Am. Chem. Soc.] Site-directed conjugation of "Clicked" glycopolymers to form glycoprotein mimics: Binding to mammalian lectin and induction of immunological function
作者：GENG, J; MANTOVANI, G; TAO, L; et al.
關(guān)鍵字：glycopolymer, click, ATRP
論文來(lái)源：期刊
具體來(lái)源：J. Am. Chem. Soc., 2007, 129 (49), pp 15156–15163
發(fā)表時(shí)間：2007年
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 (Mn = 8−30 kDa; Mw/Mn = 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.