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Proceedings Paper

A photophysical study of two fluorogen-activating proteins bound to their cognate fluorogens
Author(s): Tiziano Gaiotto; Hau B. Nguyen; Jaemyeong Jung; Gnana S. Gnanakaran; Jurgen G. Schmidt; Geoffrey S. Waldo; Andrew M. Bradbury; Peter M. Goodwin
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Paper Abstract

We are exploring the use of fluorogen-activating proteins (FAPs) as reporters for single-molecule imaging. FAPs are single-chain antibodies selected to specifically bind small chromophoric molecules termed fluorogens. Upon binding to its cognate FAP the fluorescence quantum yield of the fluorogen increases giving rise to a fluorescent complex. Based on the seminal work of Szent-Gyorgyi et al. (Nature Biotechnology, Volume 26, Number 2, pp 235-240, 2008) we have chosen to study two fluorogen-activating single-chain antibodies, HL1.0.1-TO1 and H6-MG, bound to their cognate fluorogens, thiazole orange and malachite green derivatives, respectively. Here we use fluorescence correlation spectroscopy to study the photophysics of these fluorescent complexes.

Paper Details

Date Published: 11 February 2011
PDF: 10 pages
Proc. SPIE 7905, Single Molecule Spectroscopy and Imaging IV, 79050O (11 February 2011); doi: 10.1117/12.875418
Show Author Affiliations
Tiziano Gaiotto, Los Alamos National Lab. (United States)
Hau B. Nguyen, Los Alamos National Lab. (United States)
Jaemyeong Jung, Los Alamos National Lab. (United States)
Gnana S. Gnanakaran, Los Alamos National Lab. (United States)
Jurgen G. Schmidt, Los Alamos National Lab. (United States)
Geoffrey S. Waldo, Los Alamos National Lab. (United States)
Andrew M. Bradbury, Los Alamos National Lab. (United States)
Peter M. Goodwin, Los Alamos National Lab. (United States)


Published in SPIE Proceedings Vol. 7905:
Single Molecule Spectroscopy and Imaging IV
Jörg Enderlein; Zygmunt Karol Gryczynski; Rainer Erdmann, Editor(s)

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