@booklet {235363,
	title = {Structure-based virtual screening suggests inhibitors of 3-Chymotrypsin-Like Protease of SARS-CoV-2 from Vernonia amygdalina and Occinum gratissimum},
	journal = {Computers in Biology and Medicine},
	volume = {136},
	year = {2021},
	note = {<p>Export Date: 24 May 2024; Cited By: 17</p>
},
	month = {2021},
	abstract = {<p>Antiviral culinary plants are potential bioresources for preventive nutraceuticals and/or antiviral drugs in COVID-19. Structure-based virtual screening was undertaken to screen 173 compounds previously reported from Vernonia amygdalina and Occinum gratissimum for direct interaction with the active site of the 3-Chymotrypsin-Like Protease (3CLpro) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Based on docking scores and comparison with reference inhibitors, a hit-list of 10 top phytocompounds was defined, which also had strong interactions with the catalytic centre of 3CLpro from three related strains of coronavirus (SARS-CoV, MERS-CoV, HKU4). Among these, six compounds (neoandrographolide, vernolide, isorhamnetin, chicoric acid, luteolin, and myricetin) exhibited the highest binding tendencies to the equilibrated conformers of SARS-CoV-2 3CLpro in an in-depth docking analysis to 5 different representative conformations from the cluster analysis of the molecular dynamics simulation (MDS) trajectories of the protein. In silico drug-likeness analyses revealed two drug-like terpenoids viz: neoandrographolide and vernolide as promising inhibitors of SARS-CoV-2 3CLpro. These structures were accommodated within the substrate-binding pocket; and interacted with the catalytic dyad (Cys145 and His41), the oxyanion loop (residues 138{\textendash}145), and the S1/S2 sub-sites of the enzyme active site through the formation of an array of hydrogen bonds and hydrophobic interactions. Molecular dynamics simulation and binding free energy calculation revealed that the terpenoid-enzyme complexes exhibit strong interactions and structural stability. Therefore, these compounds may stabilize the conformation of the flexible oxyanion loop; and thereby interfere with the tetrahedral oxyanion intermediate formation during the proteolytic activity of the enzyme. {\textcopyright} 2021 Elsevier Ltd</p>
},
	url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85111287561\&doi=10.1016\%2fj.compbiomed.2021.104671\&partnerID=40\&md5=4fa37c6f438b67e0291f891015a29ad2},
	author = {Gyebi, G.A. and Elfiky, A.A. and Ogunyemi, O.M. and I. M Ibrahim and Adegunloye, A.P. and Adebayo, J.O. and Olaiya, C.O. and Ocheje, J.O. and Fabusiwa, M.M.}
}
