Development of a microtiter plate fluorescent assay for inhibition studies on the HTLV-1 and HIV-1 proteinases.

Abstract

The proteinase of human T-cell leukemia virus type-1 (HTLV-1), similar to the proteinase of human immunodeficiency virus type-1 (HIV-1), is a potential target for chemotherapy, since the virus is associated with a number of human diseases. A microtiter plate fluorescent assay was developed for the HTLV-1 and HIV-1 proteinases for direct comparison of the inhibition profiles of the enzymes. It was established that, except for Indinavir, none of the inhibitors designed against the HIV-1 proteinase were able to inhibit the HTLV-1 proteinase in the studied concentration range, while two reduced peptide bond-containing peptides having the sequence of HTLV-1 cleavage sites were inhibitors of the HTLV-1 proteinase. One of these was potent enough to be used for active site titration of the HTLV-1 proteinase.

• Authors: Péter Bagossi, János Kádas, Gabriella Miklóssy, Péter Boross, Irene T Weber, József Tözsér
• Journal: Journal of virological methods (J Virol Methods) Vol. 119 Issue 2 Pg. 87-93 (Aug 2004) ISSN: 0166-0934 [Print] Netherlands
• PMID: 15158589 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Peptides
• Indinavir
• Aspartic Acid Endopeptidases
• HIV Protease
• HTLV-1 protease

Topics

• Aspartic Acid Endopeptidases (antagonists & inhibitors, chemistry, metabolism)
• Clinical Enzyme Tests (methods)
• Fluorescence
• HIV Protease (chemistry, metabolism)
• Humans
• Indinavir (pharmacology)
• Kinetics
• Peptides (metabolism)
• Substrate Specificity