TY - JOUR
T1 - α-N-Linked glycopeptides: Conformational analysis and bioactivity as lectin ligands
AU - Marcelo, Filipa
AU - Cañada, Francisco Javier
AU - André, Sabine
AU - Colombo, Cinzia
AU - Doro, Fabio
AU - Gabius, Hans Joachim
AU - Bernardi, Anna
AU - Jiménez-Barbero, Jesús
PY - 2012/8/14
Y1 - 2012/8/14
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84863940092&partnerID=8YFLogxK
U2 - 10.1039/c2ob07135e
DO - 10.1039/c2ob07135e
M3 - Article
C2 - 22441147
AN - SCOPUS:84863940092
SN - 1477-0520
VL - 10
SP - 5916
EP - 5923
JO - Organic & Biomolecular Chemistry
JF - Organic & Biomolecular Chemistry
IS - 30
ER -