title: Efficient Conjugation of Oligosaccharides to Polymer Particles through Furan/Maleimide Diels-Alder Reaction: Application to the Capture of Carbohydrate-Binding Proteins.
abstract: Glycan-protein interactions play a crucial role in physiological and pathological events. Hence, improving the isolation of carbohydrate-binding proteins (i.e., lectins and anti-glycan antibodies) from complex media might not only lead to a better understanding of their function, but also provide solutions for public health issues, such as water contamination or the need for universal blood plasma. Here we report a rapid and efficient method for producing carbohydrate-based affinity adsorbents combining enzymatic synthesis and metal-free click chemistry. Both simple and complex glycans (maltose, blood group antigens A, B, and H) were readily modified by the addition of a furyl group at the reducing end without the need for protecting groups and were then efficiently conjugated to maleimide-activated Sepharose particles through Diels-Alder cycloaddition. These neoglycoconjugates showed high efficiency for the purification of lectins (concanavalin A and Ulex europaeus agglutinin), as well as for the capture of anti-A and anti-B blood group antibodies, opening new prospects for glycoproteomics and for the development of universal blood plasma.
authors.affiliation: Université Grenoble Alpes, CERMAV, 38000, Grenoble, France.|CNRS, CERMAV, 38000, Grenoble, France.
authors.forename: Antoine
authors.initials: A
authors.lastname: Petrelli
authors.affiliation: Université Grenoble Alpes, CERMAV, 38000, Grenoble, France.|CNRS, CERMAV, 38000, Grenoble, France.
authors.forename: Eric
authors.initials: E
authors.lastname: Samain
authors.affiliation: Université Grenoble Alpes, CERMAV, 38000, Grenoble, France.|CNRS, CERMAV, 38000, Grenoble, France.
authors.forename: Stéphanie
authors.initials: S
authors.lastname: Pradeau
authors.affiliation: Université Grenoble Alpes, CERMAV, 38000, Grenoble, France.|CNRS, CERMAV, 38000, Grenoble, France.
authors.forename: Sami
authors.initials: S
authors.lastname: Halila
authors.affiliation: Université Grenoble Alpes, CERMAV, 38000, Grenoble, France.|CNRS, CERMAV, 38000, Grenoble, France.
authors.forename: Sébastien
authors.initials: S
authors.lastname: Fort
mesh_terms: D057930:Click Chemistry; D003208:Concanavalin A / Q000737:chemistry / Q000378:metabolism; D061565:Cycloaddition Reaction; D016650:Fluorescein-5-isothiocyanate / Q000737:chemistry; D005663:Furans / Q000737:chemistry*; D037102:Lectins / Q000737:chemistry / Q000378:metabolism; D008301:Maleimides / Q000737:chemistry*; D008856:Microscopy, Fluorescence; D009844:Oligosaccharides / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry*; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000378:metabolism; D012685:Sepharose / Q000737:chemistry; D013055:Spectrophotometry, Infrared
chemical_list: D005663:Furans; D037102:Lectins; D008301:Maleimides; D009844:Oligosaccharides; D011108:Polymers; D011956:Receptors, Cell Surface; C055213:saccharide-binding proteins; D003208:Concanavalin A; C043592:maleimide; D012685:Sepharose; D016650:Fluorescein-5-isothiocyanate; C039281:furan
keywords: affinity adsorbents; bioconjugation; carbohydrates; click chemistry; lectins/immunoglobulins