Journal:JBSD:8

Docking and molecular dynamics studies of peptide inhibitors of ornithine decarboxylase: a rate-limiting enzyme for the metabolism of Fusarium solani

Ashok Sharma^[1]

Molecular Tour
Fusarium solani causes stem and fruit rot disease in Capsicum sp. causing severe losses. Use of peptides as antimicrobials has been reported earlier. The peptide designing for a specific fungus using its own protein (enzyme) may be a useful strategy for the control of disease. Polyamine biosynthesis is responsible for growth of Fusarium solani. The rate-limiting step of this process is decarboxylation of ornithine. Ornithine decarboxylase (ODC) (EC 4.1.1.17) is an enzyme that catalyzes the decarboxylation of ornithine to putrescine. Ornithine is an amino acid, whereas putrescine is a polyamine. Inhibitors of ODC having higher binding capacity than ornithine can be used for treating the plant from fungal disease. In this study, we designed 15 peptide inhibitors by the random alteration of active site residues at which ornithine binds. These inhibitors were peptides of the length of nine residues. The peptide, GLIWGNGPF showed highest docking with active site of ODC, which is four times greater than ornithine. Thus, peptides can be used as a potential inhibitor to block the pathway responsible for the growth of the pathogen.