Structural dynamics and modeling of curcin protein: docking against pterin derivatives

Jatropha species have been widely targeted for its use in oil and biodiesel production. The extraction of oil and biodiesel has been curbed due to the presence of curcin, a toxalbumin that can execute detailed toxic compounds . In silico approaches were undertaken to analyse the inhibition of curcin via pterin inhibitors, which show the structural similarities to ricin inhibitors. The identification of actual residues of predicted active sites, involved in binding with the ligands was accurately confirmed by molecular docking analysis. Among the eleven ligands screened in the present study, particularly, the folic acid showed the maximum docking score, which confirmed their hydrophobic site, hydrogen-bond donor and hydrogen-bond acceptor of folic acid, which could render the optimal biological function through inhibition of curcin. Graphic abstract