Conformational behavior of α-d-mannopyranosyl-(1→6)-α,β-d-mannose complexed with two mannose-binding plant lectins, Allium sativam agglutinin I and concanavalin A, using NMR and molecular modeling techniques Original Research Article

Herein, we report the intrinsic conformational preferences of α-d-Manp-(1→6)-α,β-d-Manp, (1) in the free state and as two (ASAI and ConA) lectin-bound forms. NMR spectroscopy and molecular dynamics techniques are used as 3D-structural determination tools. In free form disaccharide 1 displays a fair amount of conformational freedom, with one major (ϕ/ψ 95 ± 30°/195 ± 20°) and one minor (95 ± 30°/70 ± 20°) conformations around the glycosidic linkage and around the ω angle, both the gg and gt rotamers are almost equally populated. This is a first report of a three-dimensional structure of 1 bound with ASAI. Both lectins recognize a major ϕ/ψ 95 ± 30°/200 ± 30° conformer with the ligand showing more flexibility in the binding site of ConA. Comparison of the mode of binding of the two lectins explains the differences in observed specificities.