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8 July 2015 Principles and application of intrinsic Förster resonance energy transfer (iFRET) for label-free detection of native proteins
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Proceedings Volume 9523, International Conference on Nano-Bio Sensing, Imaging, and Spectroscopy 2015; 952306 (2015) https://doi.org/10.1117/12.2189166
Event: International Conference on Nano-Bio Sensing, Imaging, and Spectroscopy 2015, 2015, Jeju, Korea, Republic of
Abstract
Tryptophan residues in proteins of interest were evaluated as FRET donors to facilitate the development of a label-free protein detection system, coined "intrinsic Förster (or fluorescence) resonance energy transfer (iFRET)". iFRET fluorescence probes, composed of an efficient and tryptophan-specific FRET acceptor in addition to a target protein-specific ligand, selectively bind to the target proteins thereby enabling Förster resonance energy transfer between the protein tryptophan residues and the iFRET probe. We have developed efficient iFRET acceptor fluorophores and a deep UV microscope, which were successfully applied to detect native target proteins in live cells.
© (2015) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Hyo Jin Kang, Ju Hwan Kim, Amar B. T. Ghisaidoobe, and Sang J. Chung "Principles and application of intrinsic Förster resonance energy transfer (iFRET) for label-free detection of native proteins", Proc. SPIE 9523, International Conference on Nano-Bio Sensing, Imaging, and Spectroscopy 2015, 952306 (8 July 2015); https://doi.org/10.1117/12.2189166
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