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Proceedings Paper

Determination of multiple analytes using a fiber optic biosensor based on fluorescence energy transfer
Author(s): Richard B. Thompson; Zhengfang Ge; Marcia W. Patchan; Carol A. Fierke; Keith A. McCall; Daniel Elbaum; David W. Christianson
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Paper Abstract

Recently, we have developed a biosensor for zinc based on the very tight binding of this metal by the enzyme carbonic anhydrase, which requires Zn(II) for catalysis. We were able to transduce the binding of the metal as a change in fluorescence intensity or lifetime by use of a colored inhibitor whose metal-dependent binding permits fluorescence resonance energy transfer (Forster transfer) to occur. We have extended this concept to include other metals and other analytes which may be bound in the native (or mutant) enzyme active site with a concomitant color change; the color change is transduced as a change in energy transfer efficiency. We have also recently demonstrated a similar approach, wherein the presence of a metal ion in the binding site is transduced as a change in fluorescence anisotropy. Results in cuvettes and with fiber optic sensors are shown.

Paper Details

Date Published: 1 April 1996
PDF: 10 pages
Proc. SPIE 2680, Ultrasensitive Biochemical Diagnostics, (1 April 1996); doi: 10.1117/12.237624
Show Author Affiliations
Richard B. Thompson, Univ. of Maryland/Baltimore School of Medicine (United States)
Zhengfang Ge, Univ. of Maryland/Baltimore School of Medicine (United States)
Marcia W. Patchan, Univ. of Maryland/Baltimore School of Medicine (United States)
Carol A. Fierke, Duke Univ. Medical Ctr. (United States)
Keith A. McCall, Duke Univ. Medical Ctr. (United States)
Daniel Elbaum, Univ. of Pennsylvania (United States)
David W. Christianson, Univ. of Pennsylvania (United States)


Published in SPIE Proceedings Vol. 2680:
Ultrasensitive Biochemical Diagnostics
Gerald E. Cohn; Steven A. Soper; C. H. Winston Chen, Editor(s)

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