ORGN 9 |
| Reporter molecules that relay information about chemical transformations via an optical response enable monitoring and imaging of these processes in complex systems, such as live cells. Phosphorylation of proteins and peptides stands out among post-translational modifications as the predominant mechanism of cellular signaling. As part of a program aimed at sensing chemical and enzymatic transformations via optical probes, we have developed an optical switching platform based on lanthanide-peptide conjugates, the metal-centered luminescence of which is gated as a function of the peptide's phosphorylation state. Phosphatase-catalyzed dephosphorylation of a dipeptide conjugate is readily observable by a ratiometric optical response. A dramatic change in luminescence lifetime accompanies this transformation as well; an increase from 0.7 ms to 1.5 ms is observed upon dephosphorylation. The long luminescence lifetimes of these probes highlights another feature of this platform, and demonstrates their potential usefulness as enzyme reporters in complex cellular environments. |
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Biologically-Related Molecules and Processes
8:00 AM-12:00 PM, Sunday, March 25, 2007 McCormick Place East -- Room E350, Level 3, Oral
Division of Organic Chemistry |