Unusual enhancement of dye luminescence by exciton resonance of J-Aggregates

Sorokin, A. V.; Ropakova, I. Yu.; Grankina, Irina I.; Borovoy, I. A.; Yefimova, Svetlana; Malyukin, Yuri

doi:10.1016/j.optmat.2019.109263

Cited by 3 publications

(1 citation statement)

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“…We note that although the development of functional multifluorophore architectures with high absorbance has begun more than a decade ago and currently expanded to DNA assemblies, viral capsids, protein templates, polymers, dendrimers, quantum dots, and antibodies, − only very recently, other reports have emerged on the occurrence and/or mechanisms of radiation brightening via interfluorophore coupling. , Moreover, while super-radiant molecular aggregates have been extensively studied in relation to coherent energy transfer, − they are qualitatively different from the virus-templated systems discussed here. The nearest-neighbor distance in virus-templated fluorophores is an order of magnitude greater than in molecular aggregates, which precludes the same coupling mechanism.…”

Section: Introductionmentioning

confidence: 80%

Subset of Fluorophores Is Responsible for Radiation Brightening in Viromimetic Particles

et al. 2021

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In certain conditions, dye-conjugated icosahedral virus shells exhibit suppression of concentration quenching. The recently observed radiation brightening at high fluorophore densities has been attributed to coherent emission, i.e., to a cooperative process occurring within a subset of the virussupported fluorophores. Until now, the distribution of fluorophores among potential conjugation sites and the nature of the active subset remained unknown. With the help of mass spectrometry and molecular dynamics simulations, we found which conjugation sites in the brome mosaic virus capsid are accessible to fluorophores. Reactive external surface lysines but also those at the lumenal interface where the coat protein N-termini are located showed virtually unrestricted access to dyes. The third type of labeled lysines was situated at the intercapsomeric interfaces. Through limited proteolysis of flexible N-termini, it was determined that dyes bound to them are unlikely to be involved in the radiation brightening effect. At the same time, specific labeling of genetically inserted cysteines on the exterior capsid surface alone did not lead to radiation brightening. The results suggest that lysines situated within the more rigid structural part of the coat protein provide the chemical environments conducive to radiation brightening, and we discuss some of the characteristics of these environments.

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