In silico bioprospecting of receptors associated to act mechanism of Rondonin, an antifungal peptide from spider Acanthoscurria rondoniae haemolymph

Abstract Multiresistant fungal species are associated with the development of diseases. Thus, there is a need to develop more efficient drugs for the treatment of these etiological agents. Rondonin is a peptide isolated from the hemolymph of spiders Acanthoscurria rondoniae. Previous studies showed that this peptide presented antifungal activity against Candida sp. and Trichosporon sp. strains, acting in genetic material. However, the molecular targets involved in your biological activity have not yet been described. To determine possible targets involved in the biological activity of Rondonin using bioinformatics tools. The PharmMapper server was used to search microorganism targets for Rondonin. The PatchDock server was used to perform molecular docking. UCSF Chimera software was used to evaluate these intermolecular interactions. In addition, the I-TASSER server was used to predict the target ligand sites. In the end, all predictions were contrasted with the sites previously described in the literature. Rondonin was consistent with the ligand sites of the following targets: outer membrane proteins F (id:1MPF) and A (id:1QJP), responsible for allowing the passage of small molecules through the plasmatic membrane, subunit of the flavoprotein fumarate reductase (id:1D4E), responsible for the metabolism of nitrogenous bases, and ATP-dependent Holliday DNA helicase junction (id:1IN4), associated with histone proteins that fold the genetic material. These interactions corroborate previous in vitro studies on Rondonin, which acts on fungal genetic material without plasmatic membrane rupture. Therefore, the bioprospecting methods used in this research were considered satisfactory since they showed agreement with previous results obtained in vitro.