ArticleAntimicrobial agents and chemotherapy1998
Dual inhibition of human rhinovirus 2A and 3C proteases by homophthalimides.
Article in Antimicrobial agents and chemotherapy, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 35 citations in OpenAlex.
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- Structure-activity relationship of pyrrolyl diketo acid derivatives as dual inhibitors of HIV-1 integrase and reverse transcriptase ribonuclease H domain.Journal of medicinal chemistry · 2015Article
- Pharmacophore modeling and docking studies on some nonpeptide-based caspase-3 inhibitors.BioMed research international · 2013Article
- The human rhinovirus: human-pathological impact, mechanisms of antirhinoviral agents, and strategies for their discovery.Medicinal research reviews · 2011Review
- An antiviral peptide inhibitor that is active against picornavirus 2A proteinases but not cellular caspases.Journal of virology · 2006Article
- Use of fluorescence resonance energy transfer for rapid detection of enteroviral infection in vivo.Applied and environmental microbiology · 2006Article
- Rapid multiserotype detection of human rhinoviruses on optically coated silicon surfaces.Journal of clinical virology : the official publication of the Pan American Society for Clinical Virology · 2001Article
- Inhibition of human rhinovirus-induced cytokine production by AG7088, a human rhinovirus 3C protease inhibitor.Antimicrobial agents and chemotherapy · 2000Article
- In vitro antiviral activity of AG7088, a potent inhibitor of human rhinovirus 3C protease.Antimicrobial agents and chemotherapy · 1999Article
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5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 2A and 3C proteases encoded by human rhinoviruses (HRVs) are attractive targets for antiviral drug development due to their important roles in viral replication. Homophthalimides were originally identified as inhibitors of rhinovirus 3C protease through our screening effort. Previous studies have indicated that the antiviral activity of certain homophthalimides exceeded their in vitro inhibitory activity against the viral 3C protease, suggesting that an additional mechanism might be involved. Reported here is the identification of homophthalimides as potent inhibitors for another rhinovirus protease, designated 2A. Several homophthalimides exhibit time-dependent inhibition of the 2A protease in the low-micromolar range, and enzyme-inhibitor complexes were identified by mass spectrometry. Compound LY343814, one of the most potent inhibitors against HRV14 2A protease, had an antiviral 50% inhibitory concentration of 4.2 microM in the cell-based assay. Our data reveal that homophthalimides are not only 3C but also 2A protease inhibitors in vitro, implying that the antiviral activity associated with these compounds might result from inactivation of both 2A and 3C proteases in vivo. Since the processing of the viral polyprotein is hierarchical, dual inhibition of the two enzymes may result in cooperative inhibition of viral replication. On the basis of the current understanding of their enzyme inhibitory mechanism, homophthalimides, as a group of novel nonpeptidic antirhinovirus agents, merit further structure-action relationship studies.
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