Open AccessInsilco Study on the Structural Characterization and Inhibitor Detection for Super Small Secreted Glycoprotein of Reston ebolavirus
Author(s) -
Uday M. Muddapur,
Priya I. Melmalagi,
Prajwal J. Kamble,
Nikita M. Ummannanavar,
Ramya Munavalli,
Amal Bahafi,
S. M. Shakeel Iqubal,
S. M. Shakeel Iqubal,
Tasneem Mohammed,
Abdul Rahman Ikbal,
Kayamkani Abedulla Khan,
Muazzam Sheriff Maqbul,
Ibrahim Ahmed Shaikh,
V. Priya
Publication year - 2021
Publication title -
journal of pharmaceutical research international
Language(s) - English
Resource type - Journals
ISSN - 2456-9119
DOI - 10.9734/jpri/2021/v33i60b34632
Subject(s) - in silico , ebolavirus , glycoprotein , ebola virus , in vitro , chemistry , virology , in vivo , binding site , ligand (biochemistry) , plasma protein binding , biology , biochemistry , virus , receptor , gene , genetics
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.