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• W2104548557 abstract "Abstract Purpose: To develop an imaging technology for protease activities in patients that could help in prognosis prediction and in design of personalized, protease-based inhibitors and prodrugs for targeted therapy. Experimental Design: Polyethylene glycol (PEG) was covalently attached to the N-terminus of a hydrophilic peptide substrate (GPLGVR) for matrix metalloproteinase (MMP) to increase hydrophilicity. PEG-peptide was then linked to a hydrophobic tetramethylrhodamine (TMR) domain and labeled with 18F to form a PEG-peptide-18F-TMR probe. Specific cleavage of the probe by MMP2 was tested in vitro by matrix-assisted laser desorption/ionization–time-of-flight (MALDI-TOF). In vivo imaging of MMP2-expressing tumors was evaluated by micro-PET. Results: The hydrophobic TMR fragment (948 Da) was specifically generated by MMP2 enzymes and MMP-expressing HT1080 cells but not control MCF-7 cells. MMP-expressing HT1080 cells and tumors selectively accumulated the hydrolyzed, hydrophobic TMR fragment at sites of protease activity. Importantly, we found that 18F-labeled probe (18F-TMR) preferentially localized in HT1080 tumors but not control MCF-7 tumors as shown by micro-PET. Uptake of the probe in HT1080 tumors was 18.4 ± 1.9-fold greater than in the MCF-7 tumors 30 minutes after injection. These results suggest that the PEG-peptide-18F-TMR probe displays high selectivity for imaging MMP activity. Conclusions: This strategy successfully images MMP expression in vivo and may be extended to other proteases to predict patient prognosis and to design personalized, protease-based inhibitors and prodrug-targeted therapies. Clin Cancer Res; 18(1); 238–47. ©2011 AACR." @default.
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• W2104548557 date "2012-01-01" @default.
• W2104548557 modified "2023-09-25" @default.
• W2104548557 title "<i>In Vivo</i> Positron Emission Tomography Imaging of Protease Activity by Generation of a Hydrophobic Product from a Noninhibitory Protease Substrate" @default.
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• W2104548557 doi "https://doi.org/10.1158/1078-0432.ccr-11-0608" @default.
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