Key result
Pharmacophore-based virtual screening identified two novel compounds, HRV-ZINC01537619 and HRV-ZINC601135028, that interact with catalytic residues of the HRV-3C protease.
Computational screening identified two novel compounds that interact with catalytic residues of the human rhinovirus 3C protease, offering potential leads for viral replication inhibition.
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Requires in vitro validation as HRV antivirals; leaves open therapeutic potential pending experimental confirmation.
Rhinovirus infections are estimated to be 70% of virus-related cold and flu-like illnesses. The disastrous impact of human rhinovirus infections costs healthcare systems billions annually. Herein, an in-house target-bound pharmacophore-based virtual screening protocol, outlined in our previous publications, was employed in identifying potential drug lead of 3C protease, based on the structural characteristics of rupintrivir. The two novel hits HRV-ZINC01537619 and HRV-ZINC601135028 may be commissioners of the new group of 3C proteases inhibitors against human rhinoviruses. Interestingly, both ZINC01537619 and ZINC601135028 interact with catalytic residues His40 and Cys147, respectively. This is a significant phenomenon which gives hope that viral replication inhibition is possible. These promising compounds now pave a fundamental new route toward the successful inhibition of the virus.
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Buthelezi et al. (2017) studied Human rhinovirus infections. HRV-ZINC01537619 and HRV-ZINC601135028 was evaluated on Binding to HRV-3C protease catalytic residues. Pharmacophore-based virtual screening identified two novel compounds, HRV-ZINC01537619 and HRV-ZINC601135028, that interact with catalytic residues of the HRV-3C protease.
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