Determinação de possíveis inibidores da ricina através do uso de docking molecular.

Abstract

Ricin is a highly toxic protein derived from a plant, Ricinuscommunis, better known as castor bean. This toxin has the ability to inactivate the ribosomes, resulting in inhibition of protein synthesis and as a consequence cell death by apoptosis. This characteristic makes ricin a potential biological weapon. The focus of this work is to find molecules that combat the action of ricin and are viable in a post-exposure treatment, since most cases of intoxication are due to accidental oral intake by small children and animals, as well as the attempt of suicide in the case of adults. In this work the potential of the molecules of baicalin, lactose and ɑ-D-gactose, as well as the isomers of baicalin and lactose in the inhibition of the action of ricin, using a computational biology (molecular docking) method, was evaluated. Among the ligands studied, baicalin as well as structural isomers demonstrated a high capacity to inhibit the ricin molecule associated with an ease of spontaneous binding, corroborating with the efficacy suggested in the literature. The data obtained for betaD-galactose showed that this molecule has the capacity to spontaneously bind to the ricin molecule, demonstrating the viability of the use of ricin inhibition, as in the literature. Lactose has demonstrated inhibitory ability, however its ability to carry out a spontaneous binding with the molecule is low, compared to the literature results it has been shown that it requires a large dosage to effect efficient inhibition. All the molecules evaluated had the capacity to inhibit ricin activity, with emphasis on baicalin.