This is an archive of papers published by the staff and faculty of Fox Chase Cancer Center. For questions about content, please contact Talbot Research Library
Last updated on
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
PMID: 17489551 URL: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17489551
AbstractDevelopment 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.
NotesLai, 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.