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Solution and <em>In silico</em> Ligand Binding Studies of <em>Cicer arietinum</em> Lectin | OMICS International | Abstract
ISSN: 2168-9652

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Research Article

Solution and In silico Ligand Binding Studies of Cicer arietinum Lectin

Madhurima S. Wakankar1, Krunal A. Patel2, Musti V. Krishnasastry3 and Sushama M. Gaikwad1*
1Division of Biochemical Sciences, National Chemical Laboratory, Pune, Maharashtra, 411008, India
2Division of Plant Tissue Culture, National Chemical Laboratory, Pune, Maharashtra, 411008, India
3National Centre for Cell Science, Pune, Maharashtra, 411007, India
*Corresponding Author : Dr. Sushama M. Gaikwad
Division of Biochemical Sciences
National Chemical Laboratory
Pune-411008, Maharashtra, India
Tel: +912025902241
Fax: +912025902648
Email: [email protected]
Received December 28, 2012; Accepted January 07, 2013; Published January 10, 2013
Citation: Wakankar MS, Patel KA, Krishnasastry MV, Gaikwad SM (2013) Solution and In silico Ligand Binding Studies of Cicer arietinum Lectin. Biochem Physiol S2:002. doi:10.4172/2168-9652.S2-002
Copyright: © 2013 Wakankar MS, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.


The recombinant lectin from Cicer arietinum (rCAL) showed complex sugar specificity and could bind only the asialo triantennary glycan from Fetuin. The thermodynamic study of binding to this glycan indicated the process to be spontaneous and exothermic. The values obtained were, ΔG as -28.56 kJ mol-1; ΔH as -43.65 kJ mol-1 and ΔS as -50.65 Jmol-1K-1 at 25°C. The presence of four hemopexin-binding domains in the gene sequence indicated possible binding to hemin. Binding of hemin as studied by fluorescence spectroscopy, yielded an association constant of 3.55 x 107 M-1. The lectin also bound spermine and thiamine with association constants of 1.55 x 104 M-1 and 5.37 x 103 M-1, respectively. In silico investigation was carried out by protein-ligand docking using AutoDock Vina software. Binding energies were calculated for each ligand and the amino acids involved in the interaction of these ligands with the rCAL homology model were identified. ASN-8 residue was found to be important in binding of hemin and spermine to rCAL.


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