Discovery of a Drug Lead Employing a Peptide Library: Inhibition of HIV-1 Tat and Viral Replication by the Tripeptide YPG-NH2

A library of the 8000 tripeptides derivable from coded amino acids was prepared in 20 sets of 400 using solid phase synthesis on a benzhydrylamine resin. The peptide mixtures, as C-terminal amides, were screened for inhibition of secreted alkaline phosphatase expression in a cellular (COS) system wh...

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Bibliographic Details
Published in:Antiviral chemistry & chemotherapy 1994-04, Vol.5 (2), p.128-129
Main Authors: Coffen, D. L., Huang, T.-N., Ramer, S. E., West, R. C., Connell, E. V., Schutt, A. D., Hsu, M.-C.
Format: Article
Language:English
Subjects:
Alkaline phosphatase
Amides
Antibiotics. Antiinfectious agents. Antiparasitic agents
Antiviral agents
Biological and medical sciences
CD4 antigen
HIV
Human immunodeficiency virus
Lymphocytes T
Medical sciences
Peptides
Pharmacology. Drug treatments
Replication
Solid phase methods
Tat gene
Tat protein
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Summary:A library of the 8000 tripeptides derivable from coded amino acids was prepared in 20 sets of 400 using solid phase synthesis on a benzhydrylamine resin. The peptide mixtures, as C-terminal amides, were screened for inhibition of secreted alkaline phosphatase expression in a cellular (COS) system wherein a transfected SeAP gene construct was under control of the HIV-1 LTR promoter, activated by the product of a cotransfected HIV Tat gene construct. Thus, YPG-NH2 was discovered as an inhibitor of HIV-1 Tat function and then shown to block HIV replication in a CD4+ T-cell line (CEM) with IC50 = 35μM.
ISSN:2040-2066
0956-3202
2040-2066
DOI:10.1177/095632029400500210