title: α-N-Linked glycopeptides: conformational analysis and bioactivity as lectin ligands.
abstract: Natural N-glycosylation involves a β-anomeric linkage connecting the sugar to one asparagine residue of the protein. We herein report NMR- and modelling-based data on glycomimetics containing α-glycosidic linkages. The bioactivity of α-Gal-containing glycopeptides has been documented by revealing binding to two plant lectins, i.e. a potent β-trefoil toxin (Viscum album agglutinin) and β-sandwich lectin (Erythrina corallodendron agglutinin), by NMR protocols. Docking provided insights into the 3D structures of the resulting complexes. These results provide the basis to introduce α-substituted neoglycopeptides to the toolbox of scaffold for the design of potent lectin inhibitors.
authors.affiliation: Chemical and Physical Biology, Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Ramiro de Maeztu 9, 28040 Madrid, Spain.
authors.forename: Filipa
authors.initials: F
authors.lastname: Marcelo
authors.forename: Francisco Javier
authors.initials: FJ
authors.lastname: Cañada
authors.forename: Sabine
authors.initials: S
authors.lastname: André
authors.forename: Cinzia
authors.initials: C
authors.lastname: Colombo
authors.forename: Fabio
authors.initials: F
authors.lastname: Doro
authors.forename: Hans-Joachim
authors.initials: HJ
authors.lastname: Gabius
authors.forename: Anna
authors.initials: A
authors.lastname: Bernardi
authors.forename: Jesús
authors.initials: J
authors.lastname: Jiménez-Barbero
mesh_terms: D004895:Erythrina / Q000737:chemistry; D006020:Glycopeptides / Q000737:chemistry* / Q000378:metabolism*; D008024:Ligands; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D037121:Plant Lectins / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D028182:Viscum album / Q000737:chemistry
chemical_list: D006020:Glycopeptides; D008024:Ligands; D037121:Plant Lectins