ArticleArchives of virology2026
A novel molecule inhibits SARS-CoV-2 RBD binding to the ACE2 receptor, blocks viral entry and exhibits antiviral activity in a murine model.
Article in Archives of virology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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13 authors.
Funding
Abstract
SARS-CoV-2 utilizes the cell surface receptor angiotensin-converting enzyme 2 (ACE2) for entry and infection in the host cell. Thus, the molecular interface of the receptor binding domain (RBD) and ACE2 is a potential clinical target for SARS-CoV-2 infection. A small molecule inhibitor of ACE2 could block the entry of SARS-CoV‐2 and its emerging variants. This study characterizes the RBD-ACE2 interaction inhibition activity and antiviral activity of GR 127935. The binding affinity of GR 127935 to ACE2 was confirmed using Surface Plasmon Resonance (SPR). The compound inhibited RBD-ACE2 interaction in the ELISA assay (IC50 = ~ 17 µM) and effectively blocked the entry of SARS-CoV-2 pseudovirus into HEK293T-ACE2-TMPRSS2 (IC50 = ~ 1.2 µM). Further, the anti-SARS-CoV-2 activity of GR 127935 was evaluated in vitro using the Vero cell line and a SARS-CoV-2 clinical isolate. The most prominent inhibition (EC50 = ~ 1.6 µM) was observed when the compound was added during the virus entry step. Finally, the GR 127935 treatment of BALB/c mice infected with the mouse-adapted strain of SARS-CoV-2 resulted in decreased viral load in the lungs along with a lower histopathology score. In summary, the GR 127935 molecule binds to ACE2, inhibits the molecular interaction between RBD and ACE2, and is effective in inhibiting virus replication. Thus, it is a promising potential therapeutic compound for treating human SARS-CoV-2 infections.
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