id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-328085-7wp18qb6	Barage, Sagar	Identification and characterization of novel RdRp and Nsp15 inhibitors for SARS-COV2 using computational approach	2020-11-06		.txt	text/plain	6052	362	51	This indicates that these compounds have a good binding affinity with RdRp. The resulting top 10 ligand conformations were evaluated for its binding mode and molecular interaction with active site residues of RdRP (Table 1 ). The first compound, namely, Chlorohexidine with binding free energy -10.11 Kcal/mol efficiently accommodated in the active site of RdRp and do molecular mimicry of nucleotides in terms of substructure interactions with RdRp residues (Figure 2(A) ). The second lead molecule, Ergotamine bound conformation, showed slight variation in the side-chain orientation with respect to Naldemedine binding in the active site of Nsp15 (Figure 4) . Thus, based on stability and molecular interaction and binding mode, Alectinib acts as lead molecule to design novel RdRp inhibitor to block the viral replication. The differences in NSP15 residues interaction with Naldemedine in simulated structure and predicted docked pose is due to flipped orientation of Naldemedine (Supporting Information Fig. S4B and Figure 4(B) ).	./cache/cord-328085-7wp18qb6.txt	./txt/cord-328085-7wp18qb6.txt