id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-260057-2m6jdvtc	Pandey, Preeti	Insights into the biased activity of dextromethorphan and haloperidol towards SARS-CoV-2 NSP6: in silico binding mechanistic analysis	2020-09-23		.txt	text/plain	7756	409	51	To explore the potential mechanisms of biased binding and activity of the two drugs, haloperidol and dextromethorphan towards NSP6, we herein utilized molecular docking–based molecular dynamics simulation studies. Our extensive analysis of the protein-drug interactions, structural and conformational dynamics, residual frustrations, and molecular switches of NSP6-drug complexes indicates that dextromethorphan binding leads to structural destabilization and increase in conformational dynamics and energetic frustrations. The selected docking conformations of NSP6 in complex with haloperidol and dextromethorphan were sampled by 100-ns MD simulation, and the dynamic stability of the complex was elucidated by calculating the Cα-RMSD values of the protein as the function of simulation time ( Figure S3A ). In conclusion, the study elucidated the detailed interaction mechanism of dextromethorphan and haloperidol to NSP6 protein and the associated structural and dynamical changes upon drug binding.	./cache/cord-260057-2m6jdvtc.txt	./txt/cord-260057-2m6jdvtc.txt