120636-88-6Relevant articles and documents
Sidechain-linked inhibitors of HIV-1 protease dimerization
Bowman, Michael J.,Chmielewski, Jean
experimental part, p. 967 - 976 (2009/08/08)
There is a great need for alternative modes of inhibition for the design of anti-HIV therapies, due to the increased resistance of HIV to currently approved drugs. A novel strategy for generating potent dimerization inhibitors of HIV-1 protease is describ
Peptide inhibitors of aspartic proteinases with hydroxyethylene isostere replacement of peptide bond. II. Preparation of pseudotetrapeptides derived from diastereoisomeric 5-amino-2-benzyl-4-hydroxy-6-phenylhexanoic acids
Litera, Jaroslav,Weber, Jan,Krizova, Ivana,Pichova, Iva,Konvalinka, Jan,Fusek, Martin,Soucek, Milan
, p. 541 - 548 (2007/10/03)
Twelve pseudotetrapeptides, Boc-NHCH(CH2Ph)CH(OH)CH2CH(CH2Ph) CO-Xaa-Phe-NH2 9-11, were prepared by [(benzotriazol-1-yl)oxy]tris(dimethylamino)phosphonium hexafluorophosphatemediated couplings of diastereoisomer
Design and synthesis of HIV protease inhibitors. Variations of the carboxy terminus of the HIV protease inhibitor L-682,679
DeSolms,Giuliani,Guare,Vacca,Sanders,Graham,Wiggins,Darke,Sigal,Zugay,Emini,Schleif,Quintero,Anderson,Huff
, p. 2852 - 2857 (2007/10/02)
A series of tetrapeptide analogues of 1 (L-682,679), in which the carboxy terminus has been shortened and modified, was prepared and their inhibitory activity measured against the HIV protease in a peptide cleavage assay. Selected examples were tested as inhibitors of virus spread in cell culture. Compound 12 was a 10-fold more potent enzyme inhibitor than 1 in vitro and 30-fold more potent in inhibiting the viral spread in cells.