A Study of the Active Site of Influenza Virus Sialidase: An Approach to the Rational Design of Novel Anti-influenza Drugs
| Autor: | Wen-Yang Wu, Hume Forrest White, Mark von Itzstein, Gaik B. Kok, Jeffrey Clifford Dyason, Michael S. Pegg, Stuart W. Oliver |
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| Rok vydání: | 1996 |
| Předmět: |
chemistry.chemical_classification
Binding Sites biology Protein Conformation Chemistry Stereochemistry Rational design Neuraminidase Active site Drug design Orthomyxoviridae Sialidase Antiviral Agents Virus chemistry.chemical_compound Enzyme Biochemistry Drug Design Molecular Probes Drug Discovery Aldonic acid biology.protein Molecular Medicine Computer Simulation Binding site |
| Zdroj: | Journal of Medicinal Chemistry. 39:388-391 |
| ISSN: | 1520-4804 0022-2623 |
| Popis: | The development of sialidase inhibitor-based potential anti-influenza drugs using rational drug design techniques has been of recent interest. The present study details an investigation of the active site of influenza virus sialidase by using the program GRID in an attempt to design more potent inhibitors in the hope they will eventually lead to anti-influenza drugs. A number of different probes (amino, carboxy, hydroxy, methyl, etc.) have been used in an effort to determine the functional groups most likely to improve the binding of the starting template 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en). The data have correctly predicted the binding regions for the carboxylate, acetamido (NH and methyl), and glycerol (OH) groups of N-acetylneuraminic acid. Moreover, the data suggest that the addition of certain functionalities (amino group) at the C-4 position should enhance the overall binding. |
| Databáze: | OpenAIRE |
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