| Literature DB >> 1588552 |
S D Young1, L S Payne, W J Thompson, N Gaffin, T A Lyle, S F Britcher, S L Graham, T H Schultz, A A Deana, P L Darke.
Abstract
A systematic investigation was undertaken to determine the role of the P1' sidechain in a series of hydroxyethylene isostere based inhibitors of HIV-1 protease. Substitution and homologation of the benzyl P1' side chain of the Phe-Phe isostere based pseudo peptides 1 (L-682,679) and 2 (L-685,434) with various heteroalkyl groups leads to a series of extremely potent inhibitors of the enzyme. Several examples of the most potent inhibitors were very effective in an ex vivo cell based viral spread assay using human H9 T-lymphocytes and the IIIb isolate of HIV-1. Compound 19 is 120 times more potent than 1 and 16 times more potent than 2 in inhibiting the spread of infection in this assay.Entities:
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Year: 1992 PMID： 1588552 DOI： 10.1021/jm00088a004
Source DB: PubMed Journal: J Med Chem ISSN： 0022-2623 Impact factor: 7.446