Journal
BIOCONJUGATE CHEMISTRY
Volume 18, Issue 4, Pages 1246-1250Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bc0603586
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Funding
- NCI NIH HHS [R21 CA114149-01, R01 CA099385-04, CA090468, R01 CA099385, K08 CA090468, CA099385, R21 CA114149, R33 CA114149-03, CA006927, R33 CA114149-02, CA114149, CA103991, P30 CA006927, R21 CA103991, CA86355, P50 CA086355, R33 CA114149] Funding Source: Medline
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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.
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