Photophysics of the blue fluorescent protein

Mauring, Koit; Krasnenko, Veera; Miller, Scott E.

doi:10.1016/j.jlumin.2006.01.144

Cited by 14 publications

(16 citation statements)

References 15 publications

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“…Note that the calculated quantum yield of PLGA-fluram (18%) (Fig. S3a †) is much higher than the values reported for fluorescent proteins such as green fluorescent protein (GFP) (7.3%) and its blue variants (7.9%), 27 and similar to other polymeric fluorescent materials such as poly(amido amine)s. 28,29 Finally, the calculated fluorescent brightness of PLGA-fluram (25056) is also much higher than that of other reported biodegradable photo-luminescent poly(lactide-co-glycolide) (BPLP-co-PLGA) (6550-19230) 30 and other frequently used small organic dyes such as Alexa Fluor 430 (8800) or DAPI (15660). The fluorescence intensities of the fabricated NCs show linear dependency on the NC concentration, and NCs can be clearly imaged with a fluorescence microscope (Fig.…”

Section: Bsa Loading Contentmentioning

confidence: 60%

PLGA protein nanocarriers with tailor-made fluorescence/MRI/PET imaging modalities

et al. 2020

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Section: Bsa Loading Contentmentioning

confidence: 60%

PLGA protein nanocarriers with tailor-made fluorescence/MRI/PET imaging modalities

et al. 2020

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“…The quantum yields of the BPLP-Cys (62.3%) and BPLP-Ser (26.0%) ( Fig. 2G and Table 1) were much higher than those reported for fluorescent proteins such as green fluorescent protein (GFP) (7.3%) and its blue variants (7.9%) (15). The emission range and quantum yields of all BPLPs are listed in Table 1.…”

Section: Resultsmentioning

confidence: 75%

“…Most of the organic dyes such as fluoresceins, rhodamines, and cyanine dyes are not used in vivo because they exhibit poor photostability and substantial cytotoxicity (11,12). Fluorescent proteins often suffer from photobleaching (13,14) and low quantum yield (15). Furthermore, the aggregation of fluorescent proteins inside cells may cause cellular toxicity (16).…”

Section: Fig 1 Labeling Of the Liposome (A)mentioning

confidence: 99%

Development of aliphatic biodegradable photoluminescent polymers

Yang

Zhang

Gautam

et al. 2009

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

219

271

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Fig. 1. Labeling of the liposome. (A)Outline of the method. Cells were rapidly frozen, freeze-fractured, and evaporated with carbon (C) and platinum/carbon (Pt/C) in vacuum. The replica of the split membrane was digested with SDS to remove noncast molecules and labeled by GST-PH. Both the cytoplasmic and exoplasmic halves of the membrane were examined. (B) Labeling of small unilamellar liposome replicas. Freeze-fracture replicas of liposomes containing 95 mol % of phosphatidylcholine (PC) and 5 mol % of phosphatidylinositol or a phosphoinositide were labeled. Only liposomes containing PI(4,5)P 2 were labeled intensely by GST-PH. A PH mutant, GST-PH (K30N, K32N), which does not bind PI(4,5)P 2, showed little labeling in the PI(4,5)P 2-containing liposome. (C) Quantification of the GST-PH labeling in the liposomes. The number of gold particles per 1 m 2 of the liposome surface is shown (blue). The labeling on the convex (green) and concave (yellow) surfaces showed equivalent results.

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“…The weak blue shifts observed with increasing pressure in most of the fluorescence spectra are consistent with a pressure-induced increase in rigidity, as calculated by Laurent et al 23 This lends further credibility to the idea that structural changes in the excited state are considerably hindered at elevated pressures, leading to less sampling of dark excited states and possibly a lower probability for radiationless transitions, resulting in higher quantum yields. 18 …”

Section: Resultsmentioning

confidence: 99%

Pressure-Induced Changes in the Fluorescence Behavior of Red Fluorescent Proteins

et al. 2012

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We present an experimental study on the fluorescence behavior of the red fluorescent proteins TagRFP-S, TagRFP-T, mCherry, mOrange2, mStrawberry, and mKO as a function of pressure up to several GPa. TagRFP-S, TagRFP-T, mOrange2, and mStrawberry show an initial increase in fluorescence intensity upon application of pressure above ambient conditions. At higher pressures, the fluorescence intensity decreases dramatically for all proteins under study, probably due to denaturing of the proteins. Small blue shifts in the fluorescence spectra with increasing pressure were seen in all proteins under study, hinting at increased rigidity of the chromophore environment. In addition, mOrange2 and mStrawberry exhibit strong and abrupt changes in their fluorescence spectra at certain pressures. These changes are likely due to structural modifications of the hydrogen bonding environment of the chromophore. The strong differences in behavior between proteins with identical or very similar chromophores highlight how the chromophore environment contributes to pressure-induced behavior of the fluorescence performance.

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Photophysics of the blue fluorescent protein

Cited by 14 publications

References 15 publications

PLGA protein nanocarriers with tailor-made fluorescence/MRI/PET imaging modalities

PLGA protein nanocarriers with tailor-made fluorescence/MRI/PET imaging modalities

Development of aliphatic biodegradable photoluminescent polymers

Pressure-Induced Changes in the Fluorescence Behavior of Red Fluorescent Proteins

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