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: sm.gaikwad@ncl.res.in |
| 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. | |
Abstract
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.
