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Genetically Engineered Proteins | |
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Products > Diagnostics/Immunoassays > Aquamax-HIV Protease Substrate Product HIV-1 protease substrate fused to Aquamax-aequorin
Application/Background
An assay for the detection of proteolytic bond cleavage and for the identification of HIV-1 protease inhibitors was developed using a fusion protein between a chosen recognition sequence for the HIV-1 protease and aequorin. This fusion protein was site-specifically immobilized on a 96-well microtiter plate. The assay was based on the change in bioluminescence signal obtained on the solid phase upon cleavage by the HIV-1 protease at the recognition site, thus releasing the aequorin label into the liquid phase. The aequorin that remains bound to the microtiter plate is then quantified. The optimized assay was used to determine activity of HIV-1 protease. Addition of inhibitors of the protease prevents cleavage at the recognition site, thereby allowing retention of aequorin on the solid phase. This strategy was used to screen for different drug inhibitors of the HIV-1 protease (1,2).
REFERENCES: 1. S. K. Deo, J. C. Lewis, and S. Daunert, "Bioluminescence Detection of Proteolytic Bond Breaking by Using Recombinant Aequorin", Anal. Biochem., 281, 87-94, 2000. 2. S. K. Deo, J. C. Lewis, and S. Daunert, "Bioluminescence Detection of Proteolytic Bond Cleavage by Using Recombinant Aequorin", in "Luminescence Biotechnology: Instruments and Applications", K. Van Dyke, C. Van Dyke, and K. Woodfork, Eds., CRC press, Boca Raton, FL, 107-119, 2002.
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