Journal
NATURE CHEMICAL BIOLOGY
Volume 3, Issue 10, Pages 668-677Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nchembio.2007.26
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Funding
- NCI NIH HHS [P01 CA072006] Funding Source: Medline
- NCRR NIH HHS [U54 RR020843] Funding Source: Medline
- NIBIB NIH HHS [R01 EB005011] Funding Source: Medline
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We have generated a series of quenched near- infrared fluorescent activity- based probes ( qNIRF- ABPs) that covalently target the papain- family cysteine proteases shown previously to be important in multiple stages of tumorigenesis. These ` smart' probes emit a fluorescent signal only after covalently modifying a specific protease target. After intravenous injection of NIRF- ABPs into mice bearing grafted tumors, noninvasive, whole- body imaging allowed direct monitoring of cathepsin activity. Importantly, the permanent nature of the probes also allowed secondary, ex vivo biochemical profiling to identify specific proteases and to correlate their activity with whole- body images. Finally, we demonstrate that these probes can be used to monitor small- molecule inhibition of protease targets both biochemically and by direct imaging methods. Thus, NIRF- ABPs are ( i) potentially valuable new imaging agents for disease diagnosis and ( ii) powerful tools for preclinical and clinical testing of small- molecule therapeutic agents in vivo.
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