TY - JOUR
AU - Kuzikov, Maria
AU - Costanzi, Elisa
AU - Reinshagen, Jeanette
AU - Esposito, Francesca
AU - Vangeel, Laura
AU - Wolf, Markus
AU - Ellinger, Bernhard
AU - Claussen, Carsten
AU - Geisslinger, Gerd
AU - Corona, Angela
AU - Iaconis, Daniela
AU - Talarico, Carmine
AU - Manelfi, Candida
AU - Cannalire, Rolando
AU - Rossetti, Giulia
AU - Gossen, Jonas
AU - Albani, Simone
AU - Musiani, Francesco
AU - Herzog, Katja
AU - Ye, Yang
AU - Giabbai, Barbara
AU - Demitri, Nicola
AU - Jochmans, Dirk
AU - Jonghe, Steven De
AU - Rymenants, Jasper
AU - Summa, Vincenzo
AU - Tramontano, Enzo
AU - Beccari, Andrea R.
AU - Leyssen, Pieter
AU - Storici, Paola
AU - Neyts, Johan
AU - Gribbon, Philip
AU - Zaliani, Andrea
TI - Identification of Inhibitors of SARS-CoV-2 3CL-Pro Enzymatic Activity Using a Small Molecule in Vitro Repurposing Screen
JO - ACS pharmacology & translational science
VL - 4
IS - 3
SN - 2575-9108
CY - Washington, DC
PB - ACS Publications
M1 - FZJ-2021-06125
SP - 1096 - 1110
PY - 2021
AB - Compound repurposing is an important strategy for the identification of effective treatment options against SARS-CoV-2 infection and COVID-19 disease. In this regard, SARS-CoV-2 main protease (3CL-Pro), also termed M-Pro, is an attractive drug target as it plays a central role in viral replication by processing the viral polyproteins pp1a and pp1ab at multiple distinct cleavage sites. We here report the results of a repurposing program involving 8.7 K compounds containing marketed drugs, clinical and preclinical candidates, and small molecules regarded as safe in humans. We confirmed previously reported inhibitors of 3CL-Pro and have identified 62 additional compounds with IC50 values below 1 μM and profiled their selectivity toward chymotrypsin and 3CL-Pro from the Middle East respiratory syndrome virus. A subset of eight inhibitors showed anticytopathic effect in a Vero-E6 cell line, and the compounds thioguanosine and MG-132 were analyzed for their predicted binding characteristics to SARS-CoV-2 3CL-Pro. The X-ray crystal structure of the complex of myricetin and SARS-Cov-2 3CL-Pro was solved at a resolution of 1.77 Å, showing that myricetin is covalently bound to the catalytic Cys145 and therefore inhibiting its enzymatic activity.
LB - PUB:(DE-HGF)16
UR - <Go to ISI:>//WOS:000662229400007
DO - DOI:10.1021/acsptsci.0c00216
UR - https://juser.fz-juelich.de/record/904555
ER -