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A microplate assay specific for the enzyme aggrecanase
Authors:Miller Jeffery A  Liu Rui-Qin  Davis Gary L  Pratta Michael A  Trzaskos James M  Copeland Robert A
Institution:The Bristol-Myers Squibb Company Pharmaceutical Research Institute, Experimental Station, Route 141 and Henry Clay Road, Wilmington, DE 19880, USA.
Abstract:We have identified a 41-residue peptide, bracketing the aggrecanase cleavage site of aggrecan, that serves as a specific substrate for this enzyme family. Biotinylation of the peptide allowed its immobilization onto streptavidin-coated plates. Aggrecanase-mediated hydrolysis resulted in an immobilized product that reveals an N-terminal neoepitope, recognized by the specific antibody BC-3. This assay is highly specific for aggrecanases; MMPs were inactive in this assay. Reduction of the peptide size below 30 amino acids resulted in a significant diminution of activity. Using the immobilized 41-residue peptide as a substrate, we have developed a 96-well microplate-based assay that can be conveniently used for high-throughput screening of samples for aggrecanase activity and for discovery of inhibitors of aggrecanase activity.
Keywords:Aggrecanase  Metalloprotease  Arthritis  Inflammatory joint disease  High-throughput screening  Assay design  Drug discovery
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