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Quantum Dot Bioconjugates as Energy Donors in Fluorescence Resonance Energy Transfer Assays

Published online by Cambridge University Press:  15 February 2011

Aaron R. Clapp ,
Igor L. Medintz ,
J. Matthew Mauro  and
Hedi Mattoussi
Aaron R. Clapp
Affiliation:
Optical Sciences Division
Igor L. Medintz
Affiliation:
Center for Bio/Molecular Science and Engineering, United States Naval Research Laboratory, Washington, DC 20375
J. Matthew Mauro
Affiliation:
Center for Bio/Molecular Science and Engineering, United States Naval Research Laboratory, Washington, DC 20375
Hedi Mattoussi
Affiliation:
Optical Sciences Division
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Abstract

Luminescent CdSe-ZnS core-shell quantum dot (QD) bioconjugates were used as energy donors in fluorescent resonance energy transfer (FRET) binding assays. The QDs were coated with saturating amounts of genetically engineered maltose binding protein (MBP) using a noncovalent immobilization process, and Cy3 organic dyes covalently attached at a specific sequence to MBP were used as energy acceptor molecules. Energy transfer efficiency was measured as a function of the MBP-Cy3/QD molar ratio for two different donor fluorescence emissions (different QD core sizes). Apparent donor-acceptor distances were determined from these FRET studies, and the measured distances are consistent with QD-protein conjugate dimensions previously determined from structural studies.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 773: Symposium N – Biomicroelectromechanical Systems (BioMEMS) , 2003 , N7.9
Copyright
Copyright © Materials Research Society 2003

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References

1. Lakowicz, J.R., Principles of Fluorescence Spectroscopy 2nd Ed. (Kluwer Academic, NY, 1999).Google Scholar
2. Bruchez, M. Jr, Moronne, M., Gin, P., Weiss, S., and Alivisatos, A.P., Science 281, 2013 (1998).Google Scholar
3. Chan, W.C.W. and Nie, S., Science 281, 2016 (1998).Google Scholar
4. Mattoussi, H., Mauro, J.M., Goldman, E.R., Anderson, G.P., Sundar, V.C., Mikulec, F.V. and Bawendi, M.G., J. Am. Chem. Soc. 122, 12142 (2000).Google Scholar
5. Murray, C.B., Norris, D.J. and Bawendi, M.G., J. Am. Chem. Soc. 115, 8706 (1993).Google Scholar
6. Dabbousi, B.O., Rodrigez-Viejo, J., Mikulec, F.V., Heine, J.R., Mattoussi, H., Ober, R., Jensen, K.J., and Bawendi, M.G., J. Phys. Chem. B101, 9463 (1997).Google Scholar
7. Goldman, E.R., Anderson, G.P., Tran, P.T., Mattoussi, H., Charles, P.T., and Mauro, J. M., Anal. Chem. 74, 841 (2002).Google Scholar
8. Jaiswal, J.K., Mattoussi, H., Mauro, J.M., and Simon, S.M., Nature Biotech. 21, 47 (2003).Google Scholar
9. Medintz, I.L., Mattoussi, H., Goldman, E.R., Clapp, A.R., and Mauro, J.M., submitted for publication (2003).Google Scholar
10. Clapp, A.R., Medintz, I.L., Mauro, J.M., and Mattoussi, H., submitted for publication (2003).Google Scholar