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Inhibitors of HIV protease: Unique non‐peptide active site templates
Author(s) -
Tait Bradley D.,
Domagala John,
Ellsworth Edmund L.,
Ferguson Donna,
Gajda Christopher,
Hupe Donald,
Lunney Elizabeth A.,
Tummino Peter J.
Publication year - 1996
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/(sici)1099-1352(199603)9:2<139::aid-jmr249>3.0.co;2-h
Subject(s) - template , protease , chemistry , peptide , human immunodeficiency virus (hiv) , combinatorial chemistry , active site , straddle , stereochemistry , biochemistry , enzyme , nanotechnology , biology , virology , materials science , finance , economics
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‐5 H ‐furan‐2‐ones, 4‐hydroxy‐5,6‐dihydropyrones, 3‐hydroxy‐cyclohex‐2‐enones, and 4‐hydroxy‐2(1 H )‐pyridinones, of which the 4‐hydroxy‐ 5,6‐dihydropyrones were found to be the most potent inhibitors of HIV‐1 protease.