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Your search keyword '"Thomas J. Prins"' showing total 3 results
Start Over Author "Thomas J. Prins" Journal bioorganic & medicinal chemistry letters
3 results on '"Thomas J. Prins"'

1. Structure-Based Design, Synthesis, and Biological Evaluation of Irreversible Human Rhinovirus 3C Protease Inhibitors. Part 7: Structure–Activity Studies of Bicyclic 2-Pyridone-Containing Peptidomimetics

Author

Ru Zhou, Theodore O. Johnson, Shella A. Fuhrman, David A. Matthews, Stephen T. Worland, Fausto Maldonado, Amy K. Patick, Leora S. Zalman, Thomas J. Prins, Peter S. Dragovich, Rose Ann Ferre, James W. Meador, Edward L. Brown, and Xinjun Hou

Subjects
Rhinovirus, Picornain 3C, Pyridones, medicine.drug_class, Stereochemistry, Peptidomimetic, Clinical Biochemistry, Pharmaceutical Science, Carboxamide, Cysteine Proteinase Inhibitors, Antiviral Agents, Biochemistry, Chemical synthesis, Cell Line, Structure-Activity Relationship, Viral Proteins, stomatognathic system, Drug Discovery, medicine, Humans, Structure–activity relationship, Serotyping, Molecular Biology, chemistry.chemical_classification, biology, Bicyclic molecule, Chemistry, Molecular Mimicry, Organic Chemistry, 3C Viral Proteases, virus diseases, Bridged Bicyclo Compounds, Heterocyclic, Cysteine Endopeptidases, Enzyme, Enzyme inhibitor, Drug Design, biology.protein, Molecular Medicine
Abstract

The structure-based design, chemical synthesis, and biological evaluation of bicyclic 2-pyridone-containing human rhinovirus (HRV) 3C protease (3CP) inhibitors are described. An optimized compound is shown to exhibit antiviral activity when tested against a variety of HRV serotypes (EC(50)'s ranging from 0.037 to 0.162 microM).

Published
2002
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2. Design and synthesis of irreversible depsipeptidyl human rhinovirus 3C protease inhibitors

Author

Stephen E. Webber, Joseph T. Marakovits, Peter S. Dragovich, Thomas J. Prins, Ru Zhou, Shella A. Fuhrman, Amy K. Patick, David A. Matthews, Caroline A. Lee, Babu Srinivasan, Terry Moran, Clifford E. Ford, Mary A. Brothers, James E.V. Harr, James W. Meador, Rose Ann Ferre, and Stephen T. Worland

Subjects
Models, Molecular, Rhinovirus, Stereochemistry, Clinical Biochemistry, Pharmaceutical Science, Microbial Sensitivity Tests, medicine.disease_cause, Antiviral Agents, Biochemistry, Chemical synthesis, Structure-Activity Relationship, Viral Proteins, Drug Discovery, medicine, Peptide bond, Structure–activity relationship, Protease Inhibitors, Protease inhibitor (pharmacology), Molecular Biology, chemistry.chemical_classification, Depsipeptide, Organic Chemistry, 3C Viral Proteases, Biological activity, Cysteine Endopeptidases, Enzyme, chemistry, Molecular Medicine, Peptides
Abstract

Novel tripeptidyl C-terminal Michael acceptors with an ester replacement of the P(2)-P(3) amide bond were investigated as irreversible inhibitors of the human rhinovirus (HRV) 3C protease (3CP). When screened against HRV serotype-14 the best compound was shown to have very good 3CP inhibition (k(obs)/[I]=270,000M(-1)s(-1)) and potent in vitro antiviral activity (EC(50)=7.0nM).

Published
2001
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3. Structure-based design of ketone-containing, tripeptidyl human rhinovirus 3C protease inhibitors

Author

Peter S. Dragovich, Ru Zhou, Stephen E. Webber, Thomas J. Prins, Annette K. Kwok, Koji Okano, Shella A. Fuhrman, Leora S. Zalman, Fausto C. Maldonado, Edward L. Brown, James W. Meador, Amy K. Patick, Clifford E. Ford, Mary A. Brothers, Susan L. Binford, David A. Matthews, Rose Ann Ferre, and Stephen T. Worland

Subjects
Ketone, Rhinovirus, Picornain 3C, Stereochemistry, medicine.drug_class, Clinical Biochemistry, Pharmaceutical Science, Carboxamide, Peptide, Cysteine Proteinase Inhibitors, medicine.disease_cause, Antiviral Agents, Biochemistry, Inhibitory Concentration 50, Structure-Activity Relationship, Viral Proteins, Drug Discovery, medicine, Humans, Molecular Biology, Cells, Cultured, chemistry.chemical_classification, biology, Organic Chemistry, 3C Viral Proteases, Ketones, In vitro, Cysteine Endopeptidases, Kinetics, Enzyme, chemistry, Enzyme inhibitor, Drug Design, biology.protein, Molecular Medicine, Oligopeptides
Abstract

Tripeptide-derived molecules incorporating C-terminal ketone electrophiles were evaluated as reversible inhibitors of the cysteine-containing human rhinovirus 3C protease (3CP). An optimized example of such compounds displayed potent 3CP inhibition activity (Ki=0.0045 μM) and in vitro antiviral properties (EC50=0.34 μM) when tested against HRV serotype-14.

Published
2000
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