Molecular Docking Studies of Kunitz Type of Soya Bean Trypsin Inhibitor from Erythrina Caffra with Curcumin and its Natural Analogues

Abstract

Proteinase inhibitors (PIs) are the natural, defense-related proteins present in the seeds of leguminous plants. PIs are the major cause of poor protein digestibility and low nutritive value of soyabean and other related leguminous plant proteins. They combine to protein digesting enzymes mainly trypsin and chymotrypsin thus disturbing protein digestion in the intestinal tract. In the present study crystal structure of Kunitz type of trypsin inhibitor from Erythrina caffra which belongs to soyabean trypsin inhibitor family (PDB ID-1TIE) is retrieved from RCSB Protein Data Bank and molecular docking studies were performed by taking Curcumin (CID 969516 ), which is a major constituent of turmeric, 6 Gingerol ( CID 442793 ),which is an active constituent of ginger and Isoeugenol ( CID 853433 ,) which is a phenylpropanoid occurs in the essential oils of plants respectively as ligands. Docking is performed by using autodock suite.  Binding energies are calculated and interactions are studied. Our findings suggest that these ligands show stable binding with the macromolecule with much lesser binding energies suggesting that curcumin and its structural analogues can be used for clinical trials in preventing pancreatic hypertrophy of rats fed on soyabean diet.