id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-331611-pwj226j0	Shrimp, Jonathan H.	An Enzymatic TMPRSS2 Assay for Assessment of Clinical Candidates and Discovery of Inhibitors as Potential Treatment of COVID-19	2020-06-23		.txt	text/plain	3894	216	45	We demonstrate effectiveness to quantify inhibition down to subnanomolar concentrations by assessing the inhibition of camostat, nafamostat and gabexate, clinically approved agents in Japan for pancreatitis due to their inhibition of trypsin-like proteases. The structurally related trypsin-like serine protease inhibitor nafamostat was shown to similarly inhibit spike protein-mediated cell fusion of MERS-CoV 7 . Herein we report the development of a TMPRSS2 fluorogenic biochemical assay and testing of clinical repurposing candidates for COVID19. To identify inhibitors of TMPRSS2 that may be used to validate its role in SARS-CoV-2 entry and potentially expedite to clinical trials, we developed a biochemical assay using active TMPRSS2 protease and a fluorogenic peptide substrate ( Figure 1B) . We developed a fluorogenic biochemical assay for measuring recombinant human TMPRSS2 activity for high-throughput screening that can be readily replicated and used to demonstrate that nafamostat is a more potent inhibitor than camostat and gabexate.	./cache/cord-331611-pwj226j0.txt	./txt/cord-331611-pwj226j0.txt