2021
DOI: 10.1088/1361-6463/ac1627
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Purcell radiative rate enhancement of label-free proteins with ultraviolet aluminum plasmonics

Abstract: The vast majority of proteins are intrinsically fluorescent in the ultraviolet, thanks to the emission from their tryptophan and tyrosine amino-acid constituents. However, the protein autofluorescence quantum yields are generally very low due to the prevailing quenching mechanisms by other amino acids inside the protein. This motivates the interest to enhance the radiative emission rate of proteins using nanophotonic structures. Although there have been numerous reports of Purcell effect and local density of o… Show more

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Cited by 9 publications
(12 citation statements)
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“…For a description of the aluminum nanoaperture influence on the fluorescence process, our group has recently published a detailed characterization using label-free proteins in the UV. 35 As shown by the data in Fig. 1, the presence of the horn reflector improves the collection efficiency, but the fluorescence excitation and emission enhancements occurring in the nanoaperture are not affected.…”
Section: Optical Performance and Fluorescence Enhancement Assessmentmentioning
confidence: 80%
See 1 more Smart Citation
“…For a description of the aluminum nanoaperture influence on the fluorescence process, our group has recently published a detailed characterization using label-free proteins in the UV. 35 As shown by the data in Fig. 1, the presence of the horn reflector improves the collection efficiency, but the fluorescence excitation and emission enhancements occurring in the nanoaperture are not affected.…”
Section: Optical Performance and Fluorescence Enhancement Assessmentmentioning
confidence: 80%
“…A separate calibration using diffusing molecules shows that the average brightness per protein is 3× lower for streptavidin as compared to βgalactosidase. 35 Although streptavidin has a 6.5× lower absolute number of tryptophan residues, their average quantum yield is estimated to be around 3.5% while it is only of 1.6% in β-galactosidase due to a higher quenching by nearby aminoacids. 18,35 The experiments on immobilized streptavidin proteins are performed using a 5 nM concentration to work in the same conditions as for Fig.…”
Section: Single Immobilized Protein Detectionmentioning
confidence: 99%
“…This is achieved because of the combination of (i) nanophotonic UV antenna to enhance the signal, (ii) detailed analysis to reduce the background intensity, and (iii) chemical photostabilizing agents to avoid fluorescence saturation. Our results provide guidelines on how to extend plasmonics into the UV regime and further develop label-free single molecule spectroscopy. ,, Earlier works using UV aluminum nanophotonics were restricted to proteins containing a large number of Trp residues such as β-galactosidase (156 Trps) , and streptavidin (24 Trps) . Here we improve the sensitivity by more than 1 order of magnitude, down to the single tryptophan level.…”
mentioning
confidence: 82%
“…Therefore, the brightness for streptavidin is not 24× higher than the brightness for TNase. The average quantum yield for a Trp residue in streptavidin was estimated to be 3.5 ± 1%, 18,36 while the quantum yield of Trp in TNase was reported to be 28 ± 2%. 2,41 With these values, the brightness for streptavidin is expected to be 24 × 3.5/28 = 3.0 ± 0.9 times higher than the TNase brightness.…”
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confidence: 99%
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