PEPTIDOMIMETIC INHIBITORS OF HUMAN-IMMUNODEFICIENCY-VIRUS PROTEASE (HIV-PR) - DESIGN, ENZYME BINDING AND SELECTIVITY, ANTIVIRAL EFFICACY, AND CELL-PERMEABILITY PROPERTIES

Authors
SAWYER TK FISHER JF HESTER JB SMITH CW TOMASSELLI AG TARPLEY WG BURTON PS HUI JO MCQUADE TJ CONRADI RA BRADFORD VS LIU L KINNER JH TUSTIN J ALEXANDER DL HARRISON AW EMMERT DE STAPLES DJ MAGGIORA LL ZHANG YZ POORMAN RA DUNN BM RAO C SCARBOROUGH PE LOWTHER WT CRAIK C DECAMP D MOON J HOWE WJ HEINRIKSON RL
Citation
Tk. Sawyer et al., PEPTIDOMIMETIC INHIBITORS OF HUMAN-IMMUNODEFICIENCY-VIRUS PROTEASE (HIV-PR) - DESIGN, ENZYME BINDING AND SELECTIVITY, ANTIVIRAL EFFICACY, AND CELL-PERMEABILITY PROPERTIES, Bioorganic & medicinal chemistry letters, 3(5), 1993, pp. 819-824
Citations number
22
Categorie Soggetti
Chemistry Inorganic & Nuclear","Chemistry Medicinal
Journal title
Bioorganic & medicinal chemistry letters → ACNP
ISSN journal
0960894X
Volume
3
Issue
5
Year of publication
1993
Pages
819 - 824
Database
ISI
SICI code
0960-894X(1993)3:5<819:PIOHP(>2.0.ZU;2-Q
Abstract
The structure-activity relationships and pharmacophore modeling aspect s of a series of HIV PR inhibitors modified at the N- and/or C-terminu s of the dipeptide isostere ChaPSI[CH(OH)CH2]Val (Cha. cyclohexylalani ne) are reported. The HIV PR binding affinity-selectivity (vs. human r enin, pepsin, and cathepsins-D and E), antiviral efficacy (HIV-1/vVK-1 infected CV-1 cells) and cellular permeabilities (Caco-2) are noted.