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Virtual Journal for Biomedical Optics

Virtual Journal for Biomedical Optics

| EXPLORING THE INTERFACE OF LIGHT AND BIOMEDICINE

  • Editor: Gregory W. Faris
  • Vol. 1, Iss. 11 — Nov. 13, 2006

Enhanced Green Fluorescent Protein (GFP) fluorescence after polyelectrolyte caging

Alberto Diaspro, Silke Krol, Barbara Campanini, Fabio Cannone, and Giuseppe Chirico  »View Author Affiliations


Optics Express, Vol. 14, Issue 21, pp. 9815-9824 (2006)
http://dx.doi.org/10.1364/OE.14.009815


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Abstract

Discovery of Green Fluorescent Protein (GFP) constituted an important improvement for living cell studies on submicron resolution allowing in vivo fluorescence labeling. We studied the photo-physical properties of single GFP molecules incorporated in a charged polyelectrolyte environment by means of single molecule spectroscopy. The fluorescence characteristics change dramatically in terms of photo-stability, lifetime and blinking behavior so that the proteins scale up to quantum dots. The reported results highlight interesting applications in the design of fluorescent markers and in the development of optical data storage architectures.

© 2006 Optical Society of America

OCIS Codes
(160.2540) Materials : Fluorescent and luminescent materials
(170.2520) Medical optics and biotechnology : Fluorescence microscopy
(190.4180) Nonlinear optics : Multiphoton processes

ToC Category:
Microscopy

History
Original Manuscript: August 11, 2006
Revised Manuscript: September 12, 2006
Manuscript Accepted: September 13, 2006
Published: October 16, 2006

Virtual Issues
Vol. 1, Iss. 11 Virtual Journal for Biomedical Optics

Citation
Alberto Diaspro, Silke Krol, Barbara Campanini, Fabio Cannone, and Giuseppe Chirico, "Enhanced Green Fluorescent Protein (GFP) fluorescence after polyelectrolyte caging," Opt. Express 14, 9815-9824 (2006)
http://www.opticsinfobase.org/vjbo/abstract.cfm?URI=oe-14-21-9815


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  29. The stabilizing and protecting effect in the polyelectrolyte matrix was also supported by chemically induced denaturation experiments. For this purpose, urea and guanidine hydrochloride were added to the proteins embedded in the polyelectrolyte layers and the disappearance of the fluorescence signals with time was recorded. For both agents a prolongation of the protein unfolding in comparison to wet silica gel-enveloped GFPmut2 was found (data not shown).

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