Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1975545 | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology | 2012 | 7 Pages |
Abstract
Talisin is a seed-storage protein from Talisia esculenta that presents lectin-like activities, as well as proteinase-inhibitor properties. The present study aims to provide new in vitro and in silico biochemical information about this protein, shedding some light on its mechanistic inhibitory strategies. A theoretical three-dimensional structure of Talisin bound to trypsin was constructed in order to determine the relative interaction mode. Since the structure of non-competitive inhibition has not been elucidated, Talisin-trypsin docking was carried out using Hex v5.1, since the structure of non-competitive inhibition has not been elucidated. The predicted non-coincidence of the trypsin binding site is completely different from that previously proposed for Kunitz-type inhibitors, which demonstrate a substitution of an Arg64 for the Glu64 residue. Data, therefore, provide more information regarding the mechanisms of non-competitive plant proteinase inhibitors. Bioassays with Talisin also presented a strong insecticide effect on the larval development of Diatraea saccharalis, demonstrating LD50 and ED50 of ca. 2.0% and 1.5%, respectively.
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Authors
Maria das Graças M. Freire, Octávio L. Franco, Carlos Eduardo G. Kubo, Ludovico Migliolo, Rodrigo H. Vargas, Caio Fernando Ramalho de Oliveira, José Roberto P. Parra, Maria Ligia R. Macedo,