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Assay Method Information |
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| | Protease Inhibition Assay |
| Description: | The assay involves the use of a HIV-1 protease peptide substrate which has been modified to contain a biotin moiety on one side and a fluorescent reporter molecule on the other side of the cleavable bond. In the presence of HIV-l protease, the substrate is rapidly cleaved into two parts. The biotinylated amino terminal fragment binds to the avidin Pandex beads while the FITC-containing carboxy1 terminal fragment is removed through the membrane. In the presence of an HIV-l protease inhibitor, the substrate does not cleave and the intact peptide binds to the beads. The resulting fluorescence indicates that no enzymatic reaction has occurred. Sample detection was performed by excitation at 485 nm and reading the resulting epifluorescence at 535 nm. |
| Affinity data for this assay | |
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