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Proceedings Paper

Optical biosensors based on direct coupling of recognition, signal transduction, and amplification
Author(s): Xuedong Song; Basil I. Swanson
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Paper Abstract

Highly sensitive, specific and reagent-free optical signal transduction methods for detection of polyvalent proteins have been developed by directly coupling distance-dependent fluorescence self-quenching and/or resonant energy transfer to the protein receptor binding events. The ganglioside GM1 as recognition unit for cholera toxin (CT) was covalently labeled with fluorophores, and then incorporated into a biomimetic membrane surface. In the case using fluorescence self-quenching as a signal transduction mechanism, the fluorescence intensity drops significantly due to aggregation of the fluorophore-labeled GM1 on a biomimetic surface. By labeling GM1 with a fluorescence energy transfer pair, aggregation of the labeled-GM1 results in a decrease in donor and an increase in acceptor fluorescence, providing a unique signature for specific protein-receptor binding. The detection systems can reliably detect less than 0.05 nM CT with fast response (less than five minutes). This approach can easily be adapted to any biosensor scheme that relies on multiple receptors or coreceptors. The methods can also be applied to investigate the kinetics and thermodynamics of the multivalent interactions.

Paper Details

Date Published: 26 February 1999
PDF: 8 pages
Proc. SPIE 3537, Electro-Optic, Integrated Optic, and Electronic Technologies for Online Chemical Process Monitoring, (26 February 1999); doi: 10.1117/12.341041
Show Author Affiliations
Xuedong Song, Los Alamos National Lab. (United States)
Basil I. Swanson, Los Alamos National Lab. (United States)

Published in SPIE Proceedings Vol. 3537:
Electro-Optic, Integrated Optic, and Electronic Technologies for Online Chemical Process Monitoring
Mahmoud Fallahi; Mahmoud Fallahi; Robert J. Nordstrom; Terry R. Todd, Editor(s)

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