1 April 1996 Determination of multiple analytes using a fiber optic biosensor based on fluorescence energy transfer
Author Affiliations +
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.
© (1996) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Richard B. Thompson, Richard B. Thompson, Zhengfang Ge, Zhengfang Ge, Marcia W. Patchan, Marcia W. Patchan, Carol A. Fierke, Carol A. Fierke, Keith A. McCall, Keith A. McCall, Daniel Elbaum, Daniel Elbaum, David W. Christianson, David W. Christianson, } "Determination of multiple analytes using a fiber optic biosensor based on fluorescence energy transfer", Proc. SPIE 2680, Ultrasensitive Biochemical Diagnostics, (1 April 1996); doi: 10.1117/12.237624; https://doi.org/10.1117/12.237624
PROCEEDINGS
10 PAGES


SHARE
Back to Top