Your browser doesn't support javascript.
De novo Design of SARS-CoV-2 Main Protease Inhibitors.
Fischer, Christian; Veprek, Nynke A; Peitsinis, Zisis; Rühmann, Klaus-Peter; Yang, Chao; Spradlin, Jessica N; Dovala, Dustin; Nomura, Daniel K; Zhang, Yingkai; Trauner, Dirk.
  • Fischer C; Department of Chemistry, New York University, 100 Washington Sq East, New York, NY, 10003, United States.
  • Veprek NA; Department of Chemistry, New York University, 100 Washington Sq East, New York, NY, 10003, United States.
  • Peitsinis Z; Department of Chemistry, Ludwig-Maximilian University Munich, Butenandtstrasse 5-13, 81377 München, Germany.
  • Rühmann KP; Department of Chemistry, New York University, 100 Washington Sq East, New York, NY, 10003, United States.
  • Yang C; Department of Chemistry, New York University, 100 Washington Sq East, New York, NY, 10003, United States.
  • Spradlin JN; Department of Chemistry, New York University, 100 Washington Sq East, New York, NY, 10003, United States.
  • Dovala D; Innovative Genomics Institute, University of California, Berkeley, Berkeley, CA, 94720, United States.
  • Nomura DK; Novartis Institutes for BioMedical Research, Emeryville, CA, 94608, United States.
  • Zhang Y; Innovative Genomics Institute, University of California, Berkeley, Berkeley, CA, 94720, United States.
  • Trauner D; Department of Chemistry, New York University, 100 Washington Sq East, New York, NY, 10003, United States.
Synlett ; 33(5): 458-463, 2021 Aug.
Article in English | MEDLINE | ID: covidwho-1472233
ABSTRACT
The COVID-19 pandemic prompted many scientists to investigate remedies against SARS-CoV-2 and related viruses that are likely to appear in the future. As the main protease of the virus, MPro, is highly conserved among coronaviruses, it has emerged as a prime target for developing inhibitors. Using a combination of virtual screening and molecular modeling, we identified small molecules that were easily accessible and could be quickly diversified. Biochemical assays confirmed a class of pyridones as low micromolar non-covalent inhibitors of the viral main protease.
Keywords
Fulltext
Print
XML
PubMed Links
Search on Google

Full text: Available Collection: International databases Database: MEDLINE Language: English Journal: Synlett Year: 2021 Document Type: Article Affiliation country: A-1582-0243

Similar

MEDLINE
LILACS
LIS
Fulltext
Print
XML
PubMed Links
Search on Google

Full text: Available Collection: International databases Database: MEDLINE Language: English Journal: Synlett Year: 2021 Document Type: Article Affiliation country: A-1582-0243