Dl. Coffen et al., DISCOVERY OF A DRUG LEAD EMPLOYING A PEPTIDE LIBRARY - INHIBITION OF HIV-1 TAT AND VIRAL REPLICATION BY THE TRIPEPTIDE YPG-NH2, Antiviral chemistry & chemotherapy, 5(2), 1994, pp. 128-129
A library of the 8000 tripeptides derivable from coded amino acids was
prepared in 20 sets of 400 using solid phase synthesis on a benzhydry
lamine resin. The peptide mixtures, as C-terminal amides, were screene
d for inhibition of secreted alkaline phosphatase expression in a cell
ular (COS) system wherein a transfected SeAP gene construct was under
control of the HIV-1 LTR promoter, activated by the product of a cotra
nsfected HIV Tat gene construct. Thus, YPG-NH2 was discovered as an in
hibitor of HIV-1 Tat function and then shown to block HIV replication
in a CD4+ T-cell line (CEM) with IC50 = 35 mu M