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Inhibitors of HIV protease: unique non-peptide active site templates
B D Tait1, J Domagala, E L Ellsworth
1Department of Chemistry, Parke-Davis Pharmaceutical Research Division of the Warner-Lambert Company, Ann Arbor, Michigan 48106, USA.
Journal of Molecular Recognition : JMR
|March 1, 1996
Abstract:
New templates were designed and prepared which straddle the active site of HIV-1 protease. These templates were designed to be "flexible scaffolds' upon which substituents could be appended to fill the pockets of HIV protease. The new templates prepared and analysed were 4-hydroxy-5H-furan-2-ones, 4-hydroxy-5,6-dihydropyrones, 3-hydroxy-cyclohex-2-enones, and 4-hydroxy-2(1H)-pyridinones, of which the 4-hydroxy-5,6-dihydropyrones were found to be the most potent inhibitors of HIV-1 protease.