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{symbol}/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{symbol}/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. © 2009 Elsevier Ltd. All rights reserved.

CHAITALI MUKHOPADHYAY

Chemistry

P MAZUMDER

University of Calcutta (informally known as Calcutta University or CU) is a collegiate public state university located in Kolkata, West Bengal, India.&nbsp;Within India it is recognized as a &quot;Five-Star University&quot; and accredited &quot;A&quot; Grade by National Assessment and Accreditation Council.

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The University of Calcutta has secured the Fifth position among the Universities of India in the prestigious &quot;Indian University Ranking 2019&quot; list, released by the NIRF of the Ministry of Human Resource Development, Government of India.

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It was established on 24 January 1857, and was one of the first institutions in Asia to be established as a multidisciplinary and Western-style university. Its alumni and faculty include several heads of state, heads of government, social reformers, prominent artists, only academy award winner and Dirac medal winner in India, many Fellows of the Royal Society and five Nobel laureates as of 2019 which is highest in South Asia.

University Of Calcutta

Carbohydrate Research

The interaction of trimannoside, a2benzyl 3, 6-di-O-(a-D-mannopyranosyl)-a-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 (a 1 → 3 and a 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

Molecular modeling and NMR studies of benzyl substituted mannosyl trisaccharide binding to two mannose-specific lectins: Allium sativam agglutinin I and Concanavalin A

Ricin B is a galactose-binding protein, which contains two binding sites. We have compared the binding properties of the two binding sites of ricin B chain toward different mono- and disaccharide ligands. The free energies of binding are calculated using the free energy perturbation simulation (thermodynamic integration method) and linear interaction energy approach using CHARMM force field. The second binding site of the protein was found to be weaker compared to the first. The details of the hydrogen-bonding scheme suggested the origin of the epimeric specificity of the protein. The reason for the weaker binding capacity of the second binding site has been addressed. © 2006 Wiley Periodicals, Inc.

Binding diversity of the two binding sites of ricin B lectin

Journal of Computational Chemistry

GROMACS: Fast, flexible, and free

ChemBioChem

Chemical Biology of the Sugar Code

Current Topics in Medicinal Chemistry

Second-Site NMR Screening and Linker Design

Encyclopedia of Computational Chemistry

GROMOS Force Field

Conformational behavior of Î±-d-mannopyranosyl-(1â†’6)-Î±,Î²-d-mannose complexed with two mannose-binding plant lectins, Allium sativam agglutinin I and concanavalin A, using NMR and molecular modeling techniques

Journal	Carbohydrate Research
Publisher	-
ISSN	0008-6215
Open Access	No