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Biotinylated Inhibitor for the Detection of Protein Activity by Stripping
Most peptide-type protease inhibitors interact with the active site of the protease. Once these inhibitors are bound to the protease, they must be removed from the protease by macro-dilution or protein denaturation. However, KNI1293 biotin, a biotinylated HIV-1 (human immunodeficiency virus type 1) protease inhibitor,1,2) can be removed (stripped) by streptavidin after binding to the protease.3) The biotinylated protease inhibitor-streptavidin binding shift phenomenon is expected to be used to study the activity of protease-related diseases.
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References
- 1) Small-Sized Human Immunodeficiency Virus Type-1 Protease Inhibitors Containing Allophenylnorstatine to Explore the S2‘ Pocket
- 2) Antimalarial activity enhancement in hydroxymethylcarbonyl (HMC) isostere-based dipeptidomimetics targeting malarial aspartic protease plasmepsin
- 3) Acquired Removability of Aspartic Protease Inhibitors by Direct Biotinylation
