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• W2041239734 abstract "The interaction of trimannoside, α−benzyl 3, 6-di-O-(α-D-mannopyranosyl)-α-D-mannopyranoside, 1 with ASAI (Allium sativam agglutinin I, garlic lectin) was studied to reveal the conformational preferences of this ligand in bound-state and detailed binding mode at atomic level. The binding phenomenon was then compared with another well-known mannose-binding lectin, ConA (Concanavalin A). Structural studies of the ligand in free state were done using NMR spectroscopy and Molecular Dynamics simulations. It is found that the substituted-trimannoside can undergo conformational transitions in solution, with one major and one minor conformation per glycosidic linkage (α 1→3 and α 1→6). On the other hand in the bound-state only one of the two major conformations was significantly populated. The role of phenyl ring in the binding process was explored. An extended binding site was observed for the trimannoside in ASAI utilizing the aromatic substituent, which is not seen in ConA. Binding data from difference absorption spectroscopy supported this fact that the binding of benzyl-substituted ligand is tighter with ASAI than ConA. © 2010 Wiley Periodicals, Inc. Biopolymers 93: 952–967, 2010." @default.
• W2041239734 created "2016-06-24" @default.
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• W2041239734 date "2010-08-25" @default.
• W2041239734 modified "2023-09-24" @default.
• W2041239734 title "Molecular modeling and NMR studies of benzyl substituted mannosyl trisaccharide binding to two mannose-specific lectins: Allium sativam agglutinin I and Concanavalin A" @default.
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• W2041239734 doi "https://doi.org/10.1002/bip.21503" @default.
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