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A simple, continuous fluorometric assay for HIV protease.

M V Toth¹, G R Marshall

¹Department of Pharmacology, Washington University School of Medicine, St. Louis, Missouri.

International Journal of Peptide and Protein Research

|December 1, 1990

Summary

Researchers developed novel fluorogenic substrates to detect human immunodeficiency virus (HIV) protease activity. This assay enables high-throughput screening for potential HIV protease inhibitors, aiding drug discovery.

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Area of Science:

Biochemistry
Molecular Biology
Drug Discovery

Background:

Human immunodeficiency virus (HIV) protease is a critical target for antiviral therapy.
Developing sensitive assays to detect protease activity is essential for identifying inhibitors.

Purpose of the Study:

To develop novel fluorogenic substrates for detecting human immunodeficiency viral protease activity.
To establish a high-throughput screening method for HIV protease inhibitors.

Main Methods:

Designed and synthesized novel fluorogenic substrates based on fluorescence energy transfer (FRET).
Utilized a hexapeptide sequence mimicking the p24/p15 cleavage site.
Incorporated 2-aminobenzoic acid as a donor and p-NO2-Phe as an acceptor for intramolecular quenching.

Main Results:

Cleavage by HIV protease released the fluorescent N-terminal tripeptide, leading to enhanced fluorescence.
An automated assay using 96-well microtiter plates and a fluorometric plate reader was established.
The assay demonstrated suitability for high-throughput screening of compounds.

Conclusions:

Novel fluorogenic substrates effectively detect HIV protease activity.
The developed automated assay facilitates efficient screening for HIV protease inhibitors.
This platform supports the search for new antiviral drugs against HIV.

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