Super small secreted glycoprotein (ssGP) is a virulent protein that plays a vital role during the Ebola viral infection. This study entails in silico structural and finding inhibitor compound for the secreted glycoprotein of Reston ebola virus (strain Philippines-96). The physical and stereochemical properties and the protein's secondary and tertiary structure were predicted initially. Later, as the predicted model was evaluated to be a reliable structure, binding pockets were predicted, and known binding ligands to similar proteins were identified. Analogue compounds to known ligands were collected and docked against ssGP. The compound with the least binding energy was identified and recommended as a potent inhibitor towards ssGP. From this study, in-vitro and in-vivo analysis was computed for the selected ligand for designing effective drugs against Reston ebolavirus.
Background: Porphyromonas gingivalis (P. gingivalis) is a primary etiologic agent of generalized aggressive and chronic forms of periodontitis. It releases toxins called 'gingipains' .
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