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Lai KS , Ho NH , Cheng JD , Tung CH
Selective fluorescence probes for dipeptidyl peptidase activity-fibroblast activation protein and dipeptidyl peptidase IV
Bioconjug Chem. 2007 Jul-Aug;18(4) :1246-50
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Development of suitable tools to assess enzyme activity directly from their complex cellular environment has a dramatic impact on understanding the functional roles of proteins as well as on the discovery of new drugs. In this study, a novel fluorescence-based chemosensor strategy for the direct readout of dipeptidase activities within intact living cells is described. Selective activity-based probes were designed to sense two important type II transmembrane serine proteases, fibroblast activation protein (FAP) and dipeptidyl peptidase IV (DPP-IV). These serine proteases have been implicated in diverse cellular activities, including blood coagulation, digestion, immune responses, wound healing, tumor growth, tumor invasion, and metastasis. Here, we validated that Ac-GPGP-2SBPO and GPGP-2SBPO probes are excellent reporters of both proteolytic activities. Furthermore, the novel probes can differentiate between FAP and DPP-IV proteolytic activities in cellular assay. Potentially, this assay platform is immediately useful for novel drug discovery.
Lai, Koon Siew Ho, Nan-Hui Cheng, Jonathan D Tung, Ching-Hsuan CA006927/CA/United States NCI CA090468/CA/United States NCI CA099385/CA/United States NCI CA103991/CA/United States NCI CA114149/CA/United States NCI CA86355/CA/United States NCI Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't United States Bioconjugate chemistry Bioconjug Chem. 2007 Jul-Aug;18(4):1246-50. Epub 2007 May 10.