Data storage based on photochromic and photoconvertible fluorescent proteins

Adam, Virgile; Mizuno, Hideaki; Grichine, Alexeï; Hotta, Jun‐ichi; Yamagata, Yutaka; Moeyaert, Benjamien; Nienhaus, G. Ulrich; Miyawaki, Atsushi; Bourgeois, Dominique; Hofkens, Johan

doi:10.1016/j.jbiotec.2010.04.001

Cited by 65 publications

(52 citation statements)

References 110 publications

(124 reference statements)

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“…2PLSM should make it possible to obtain even better optical recordings of ion concentration and cell signaling with genetically targeted sensors 5,6 . Two-photon excitation of fluorescent proteins can also be considered as potentially advantageous in the contexts of genetically targeted deep photodynamic therapy or chromophore-assisted light inactivation 6 , three-dimensional optical memory 7 , as well as superresolution (sub-diffraction limited) imaging techniques, such as stimulated emission depletion 8 , photo-activated localization microscopy, and stochastic optical reconstruction microscopy 9 .…”

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confidence: 99%

Two-photon absorption properties of fluorescent proteins

et al. 2011

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Two-photon excitation of fluorescent proteins is an attractive approach for imaging living systems. Today researchers are eager to know which proteins are the brightest, and what the best excitation wavelengths are. Here we review the two-photon absorption properties of a wide variety of fluorescent proteins, including new far-red variants, to produce a comprehensive guide to choosing the right FP and excitation wavelength for two-photon applications.Two-photon laser scanning microscopy (2PLSM) 1,2 of cells and tissues expressing fluorescent proteins is becoming a powerful tool for biological studies at different levels of organization [2][3][4] . The advantages of two-photon excitation (2PE) include reduced out-offocus photobleaching, less autofluorescence, deeper tissue penetration, and intrinsically high three-dimensional resolution 1,2 . 2PLSM should make it possible to obtain even better optical recordings of ion concentration and cell signaling with genetically targeted sensors 5,6 . Twophoton excitation of fluorescent proteins can also be considered as potentially advantageous in the contexts of genetically targeted deep photodynamic therapy or chromophore-assisted light inactivation 6 , three-dimensional optical memory 7 , as well as superresolution (subdiffraction limited) imaging techniques, such as stimulated emission depletion 8 , photoactivated localization microscopy, and stochastic optical reconstruction microscopy 9 .To fully realize the potential of 2PE of the fluorescent proteins, it is important to know their two-photon absorption (2PA) spectra, cross sections, σ 2 , and 2PE action cross sections, or brightness, σ 2 ', (σ 2 ' = σ 2 × φ, where φ is the fluorescence quantum yield). The linear, onephoton absorption (1PA) spectra and extinction coefficients of many fluorescent proteins have been described and reviewed 5,6,10 (Supplementary Table 1 online), but the 1PA properties are not sufficient to predict the key 2PA properties such as optimum excitation wavelength and maximum brightness (Box 2).Correspondence should be addressed to M.D. (drobizhev@physics.montana.edu).. 4 Present address: School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia. 5 Present address: Vollum Institute, Oregon Health and Science University, Portland, Oregon. HHS Public Access Author Manuscript Author ManuscriptAuthor Manuscript Author ManuscriptHere we present a systematic characterization of the 2PA properties of 48 different fluorescent proteins using the same experimental setup, common 2PA reference standards, and an all-optical method for measuring mature chromophore concentration 11 (Supplementary Methods online). Briefly, we use a relative fluorescence method with femtosecond excitation and coumarin 485 (Exciton), coumarin 540A (Exciton), rhodamine 610 (Exciton), fluorescein (Aldrich), and styryl 9M (Aldrich) as 2PA standards 12 , which eliminates the necessity to calibrate the laser parameters. The power dependence of the fluorescence signal was quadratic for all data ...

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Two-photon absorption properties of fluorescent proteins

et al. 2011

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“…Only RSFPs can be used for repeated measurements of protein movements in live cells (3) and for the emerging technique of optical lock-in detection (OLID) (4). Moreover, RSFPs possess all the fundamental requirements to be useful for rewritable ultrahigh density optical data storage (5,6). In addition, RSFPs demonstrate great potential for use in recently developed superresolution microscopy techniques, such as reversible saturable optical fluorescence transition (RESOLFT) microscopy with ultralow light intensities (7,8) and photoactivated localization microscopy (PALM) (9) or stochastic optical reconstruction microscopy (STORM) (10), or fluorescence photoactivation localization microscopy (FPALM) (11) [collectively referred as (F)PALM/STORM].…”

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A unique series of reversibly switchable fluorescent proteins with beneficial properties for various applications

Chang

Zhang

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

118

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Reversibly switchable fluorescent proteins (RSFPs) have attracted widespread interest for emerging techniques including repeated tracking of protein behavior and superresolution microscopy. Among the limited number of RSFPs available, only Dronpa is widely employed for most cell biology applications due to its monomeric and other favorable photochemical properties. Here we developed a series of monomeric green RSFPs with beneficial optical characteristics such as high photon output per switch, high photostability, a broad range of switching rate, and pH-dependence, which make them potentially useful for various applications. One member of this series, mGeos-M, exhibits the highest photon budget and localization precision potential among all green RSFPs. We propose mGeos-M as a candidate to replace Dronpa for applications such as dynamic tracking, dual-color superresolution imaging, and optical lock-in detection.

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“…Unlike photoconvertible proteins, which can create red fluorescent patterns irreversibly created by light, photoswitchable FPs allow for multiple writing cycles [44]. 2D data writing has been performed with Dronpa and IrisFP coated on a surface, and 3D data writing in crystals of IrisFP and other EosFP mutants [27, 45].…”

Section: Applicationsmentioning

confidence: 99%

Photoswitchable fluorescent proteins: ten years of colorful chemistry and exciting applications

Zhou

Lin

2013

Current Opinion in Chemical Biology

157

139

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Reversibly photoswitchable fluorescent proteins (RSFPs) are fluorescent proteins whose fluorescence, upon excitation at a certain wavelength, can be switched on or off by light in a reversible manner. In the last ten years, many new RSFPs have been developed and novel applications in cell imaging discovered that rely on their photoswitching properties. This review will describe research on the mechanisms of reversible photoswitching and recent applications using RSFPs. While cis-trans isomerization of the chromophore is believed to be the general mechanism for most RSFPs, structural studies reveal diversity in the details of photoswitching mechanisms, including different effects of protonation, chromophore planarity, and pocket flexibility. Applications of RSFPs include new types of live-cell superresolution imaging, tracking of protein movements and interactions, information storage, and optical control of protein activity.

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Data storage based on photochromic and photoconvertible fluorescent proteins

Cited by 65 publications

References 110 publications

Two-photon absorption properties of fluorescent proteins

Two-photon absorption properties of fluorescent proteins

A unique series of reversibly switchable fluorescent proteins with beneficial properties for various applications

Photoswitchable fluorescent proteins: ten years of colorful chemistry and exciting applications

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