Please use this identifier to cite or link to this item:
|Title:||Inhibitor fingerprinting of metalloproteases using microplate and microarray platforms: An enabling technology in Catalomics|
|Citation:||Lee, W.L., Li, J., Uttamchandani, M., Sun, H., Yao, S.Q. (2007-09). Inhibitor fingerprinting of metalloproteases using microplate and microarray platforms: An enabling technology in Catalomics. Nature Protocols 2 (9) : 2126-2138. ScholarBank@NUS Repository. https://doi.org/10.1038/nprot.2007.305|
|Abstract:||One of the most fundamental properties of an enzyme is its selectivity, a property that has proved highly challenging to understand. Recent developments offer methodologies to rapidly establish activity-dependent profiles of enzymes. In this protocol, we describe methods to elucidate inhibitor fingerprints of enzymes. By taking advantage of well-defined small-molecule inhibitor libraries and the screening throughput offered from microplate and microarray platforms, we provide step-by-step application of the methodology toward the global characterization of metalloproteases, an important class of enzymes involved in numerous diseases and cellular processes. The same strategy is nonetheless applicable to virtually any given enzyme class, provided suitable experimental design and chemical inhibitor libraries are carefully implemented. We are able to routinely fingerprint as many as 2,000 independent enzyme interactions on the microplate platform within a span of ∼7 h; however, the same throughput is attained within 5 h on the microarray platform.|
|Source Title:||Nature Protocols|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Mar 21, 2019
WEB OF SCIENCETM
checked on Mar 12, 2019
checked on Mar 16, 2019
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.