id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-330110-pamxy4av	Teissier, Elodie	Mechanism of Inhibition of Enveloped Virus Membrane Fusion by the Antiviral Drug Arbidol	2011-01-25		.txt	text/plain	9268	438	48	Interestingly, apparent binding affinities between lipids and tryptophan residues are comparable with those of Arb IC50 of the hepatitis C virus (HCV) membrane fusion. By combining surface plasmon resonance, fluorescence and NMR spectroscopy approaches, we showed that Arb directly interacts with the phospholipid membrane interface, with an affinity in the micromolar range, comparable to the concentration inhibiting HCVpp membrane fusion by 50% (IC50). Altogether our results demonstrate that Arb interacts with the polar head of phospholipid membranes and protein motifs enriched in aromatic residues, suggesting that the inhibitory activity of Arb on HCV entry and fusion could involve both types of interactions. Conversely, Arb inhibition of HCVpp membrane fusion, as assessed by a in vitro model system where the only proteins present are the viral glycoproteins, could merely reflect the interaction of Arb on lipids and/or on motifs present in HCV glycoproteins of any genotype.	./cache/cord-330110-pamxy4av.txt	./txt/cord-330110-pamxy4av.txt