Molecular characterization of ebselen binding activity to SARS-CoV-2 main protease
Year: 2020
Type: article
Abstract: activity. We find that it exhibits a distinct affinity for the catalytic region. Our results reveal a higher-affinity, previously unknown binding site localized between the II and III domains of the protein. A detailed strain analysis indicates that, on such a site, ebselen exerts a pronounced allosteric effect that regulates catalytic site access through surface-loop interactions, thereby inducing a reconfiguration of water hotspots. Together, these findings highlight the promise of ebselen as a repurposed drug against SARS-CoV-2.
Source: Science Advances
Institutions: University of Chicago, Argonne National Laboratory
Language: English
Subfield: Infectious Diseases
Field: Medicine
Domain: Health Sciences
Open Access status: gold
Estimated APC paid: $4,500
Funders: National Science Foundation, U.S. Department of Energy, University of Chicago, Office of Science, Multidisciplinary University Research Initiative, National Institute of Biomedical Imaging and Bioengineering, Division of Materials Research, Division of Emerging Frontiers in Research and Innovation, Division of Molecular and Cellular Biosciences, Basic Energy Sciences
Awards: G1256303824, Graduate Program in Biophysical Sciences at the University of Chicago, G2879087551, MRI: Acquisition of a high-performance GPU-based computer for advanced multiscale materials modeling, EFRI CEE: Epigenomic Regulation Over Multiple Length Scales: Understanding Chromatin Modifications Through Label Free Imaging and Multi-Scale Modeling, Chromatin Structure and Dynamics from Nanometer to Micrometer Length Scales, G7820774471
OpenAlex ID: W3027085332