Protein Kinase-Actuated Resonance Energy Transfer in Quantum Dot−Peptide Conjugates
- 12 July 2010
- journal article
- Published by American Chemical Society (ACS) in ACS Nano
- Vol. 4 (8), 4915-4919
- https://doi.org/10.1021/nn101293s
Abstract
Bioconjugates of quantum dot nanocrystals possess unique optical properties that allow them to serve as exceptional biological imaging and sensing reagents. Protein kinases are an important family of enzymes that phosphorylate serine, threonine, or tyrosine side chains and are critical in cell signaling and cancer biology, but despite their biomedical and pharmaceutical significance, their activity has been little explored using quantum dot technology. We demonstrate that self-assembled peptide-quantum dot conjugates can serve as surrogate substrates in a simple homogeneous assay for protein kinase activity. Enzymatic phosphorylation of the peptide-conjugates is detected by means of a complementary FRET-acceptor labeled antiphosphotyrosine antibody, with formation of the immunocomplex resulting in energy transfer between the quantum dot and FRET acceptor molecules. This approach should facilitate the development of new assays for protein kinases and other enzymes based on quantum dot FRET donors.Keywords
This publication has 24 references indexed in Scilit:
- Cell cycle kinases as therapeutic targets for cancerNature Reviews Drug Discovery, 2009
- Protein Nanoparticles Engineered to Sense Kinase Activity in MRIJournal of the American Chemical Society, 2009
- Quantum dot-based resonance energy transfer and its growing application in biologyPhysical Chemistry Chemical Physics, 2008
- Examining Förster Energy Transfer for Semiconductor Nanocrystalline Quantum Dot Donors and AcceptorsThe Journal of Physical Chemistry C, 2008
- Measuring the tyrosine kinase activity: a review of biochemical and cellular assay technologiesExpert Opinion on Drug Discovery, 2008
- Nanoparticle Self‐Assembly Directed by Antagonistic Kinase and Phosphatase ActivitiesAdvanced Materials, 2007
- Protease-Triggered Dispersion of Nanoparticle AssembliesJournal of the American Chemical Society, 2007
- High‐Throughput Screening for Kinase InhibitorsChemBioChem, 2005
- Quantitative methods for the analysis of protein phosphorylation in drug developmentExpert Review of Proteomics, 2004
- Protein kinases — the major drug targets of the twenty-first century?Nature Reviews Drug Discovery, 2002