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The vast majority of proteins are intrinsically fluorescent in theultraviolet, thanks to the emission from their tryptophan and tyrosineamino-acid constituents. However, the protein autofluorescence quantum yieldsare generally very low due to the prevailing quenching mechanisms by otheramino acids inside the protein. This motivates the interest to enhance theradiative emission rate of proteins using nanophotonic structures. Althoughthere have been numerous reports of Purcell effect and local density of opticalstates (LDOS) control in the visible range using single dipole quantumemitters, the question remains open to apply these concepts in the UV on realproteins containing several tryptophan and tyrosine amino acids arranged in ahighly complex manner. Here, we report the first complete characterization ofthe Purcell effect and radiative rate enhancement for the UV intrinsicfluorescence of label-free \b{eta}-galactosidase and streptavidin proteins inplasmonic aluminum nanoapertures. We find an excellent agreement with acalibration performed using a high quantum yield UV fluorescent dye.Demonstrating and intensifying the Purcell effect is essential for theapplications of UV plasmonics and the label-free detection of single proteins.

Purcell radiative rate enhancement of label-free proteins with ultraviolet aluminum plasmonics