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Proceedings Paper

Principles and application of intrinsic Förster resonance energy transfer (iFRET) for label-free detection of native proteins
Author(s): Hyo Jin Kang; Ju Hwan Kim; Amar B. T. Ghisaidoobe; Sang J. Chung
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Paper 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.

Paper Details

Date Published: 8 July 2015
PDF: 4 pages
Proc. SPIE 9523, International Conference on Nano-Bio Sensing, Imaging, and Spectroscopy 2015, 952306 (8 July 2015); doi: 10.1117/12.2189166
Show Author Affiliations
Hyo Jin Kang, Dongguk Univ. (Korea, Republic of)
Ju Hwan Kim, Dongguk Univ. (Korea, Republic of)
Amar B. T. Ghisaidoobe, Dongguk Univ. (Korea, Republic of)
Sang J. Chung, Dongguk Univ. (Korea, Republic of)

Published in SPIE Proceedings Vol. 9523:
International Conference on Nano-Bio Sensing, Imaging, and Spectroscopy 2015
Donghyun Kim; Min-Gon Kim; Seung-Han Park, Editor(s)

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