Oxygen-Insensitive Aggregates of Pt(II) Complexes as Phosphorescent Labels of Proteins with Luminescence Lifetime-Based Readouts
The synthesis and photophysical properties of a tailored Pt(II) complex are presented. The phosphorescence of its monomeric species in homogeneous solutions is quenched by interaction with the solvent and therefore absent even upon deoxygenation. However, aggregation-induced shielding from the envir...
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2018
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19448244_v10_n29_p24361_Delcanale http://hdl.handle.net/20.500.12110/paper_19448244_v10_n29_p24361_Delcanale |
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paper:paper_19448244_v10_n29_p24361_Delcanale2023-06-08T16:32:25Z Oxygen-Insensitive Aggregates of Pt(II) Complexes as Phosphorescent Labels of Proteins with Luminescence Lifetime-Based Readouts donor-acceptor energy transfer labeling photophysics PLIM Pt(II) complex spectroscopy time-gated spectroscopy Aggregates Binary alloys Body fluids Degrees of freedom (mechanics) Energy transfer Excited states Fluorophores Labeling Molecular oxygen Phosphorescence Proteins Spectroscopy Donor acceptors Excited state lifetimes Phosphorescence lifetime Photophysical properties Photophysics PLIM Pt complexes Reactive oxygen species Platinum compounds The synthesis and photophysical properties of a tailored Pt(II) complex are presented. The phosphorescence of its monomeric species in homogeneous solutions is quenched by interaction with the solvent and therefore absent even upon deoxygenation. However, aggregation-induced shielding from the environment and suppression of rotovibrational degrees of freedom trigger a phosphorescence turn-on that is not suppressed by molecular oxygen, despite possessing an excited-state lifetime ranging in the microsecond scale. Thus, the photoinduced production of reactive oxygen species is avoided by the suppression of diffusion-controlled Dexter-type energy transfer to triplet molecular oxygen. These aggregates emit with the characteristic green luminescence profile of monomeric complexes, indicating that Pt-Pt or excimeric interactions are negligible. Herein, we show that these aggregates can be used to label a model biomolecule (bovine serum albumin) with a microsecond-range luminescence. The protein stabilizes the aggregates, acting as a carrier in aqueous environments. Despite spectral overlaps, the green phosphorescence can be separated by time-gated detection from the dominant autofluorescence of the protein arising from a covalently bound green fluorophore that emits in the nanosecond range. Interestingly, the aggregates also acted as energy donors able to sensitize the emission of a fraction of the fluorophores bound to the protein. This resulted in a microsecond-range luminescence of the fluorescent acceptors and a shortening of the excited-state lifetime of the phosphorescent aggregates. The process that can be traced by a 1000-fold increase in the acceptor's lifetime mirrors the donor's triplet character. The implications for phosphorescence lifetime imaging are discussed. © 2018 American Chemical Society. 2018 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19448244_v10_n29_p24361_Delcanale http://hdl.handle.net/20.500.12110/paper_19448244_v10_n29_p24361_Delcanale |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
donor-acceptor energy transfer labeling photophysics PLIM Pt(II) complex spectroscopy time-gated spectroscopy Aggregates Binary alloys Body fluids Degrees of freedom (mechanics) Energy transfer Excited states Fluorophores Labeling Molecular oxygen Phosphorescence Proteins Spectroscopy Donor acceptors Excited state lifetimes Phosphorescence lifetime Photophysical properties Photophysics PLIM Pt complexes Reactive oxygen species Platinum compounds |
| spellingShingle |
donor-acceptor energy transfer labeling photophysics PLIM Pt(II) complex spectroscopy time-gated spectroscopy Aggregates Binary alloys Body fluids Degrees of freedom (mechanics) Energy transfer Excited states Fluorophores Labeling Molecular oxygen Phosphorescence Proteins Spectroscopy Donor acceptors Excited state lifetimes Phosphorescence lifetime Photophysical properties Photophysics PLIM Pt complexes Reactive oxygen species Platinum compounds Oxygen-Insensitive Aggregates of Pt(II) Complexes as Phosphorescent Labels of Proteins with Luminescence Lifetime-Based Readouts |
| topic_facet |
donor-acceptor energy transfer labeling photophysics PLIM Pt(II) complex spectroscopy time-gated spectroscopy Aggregates Binary alloys Body fluids Degrees of freedom (mechanics) Energy transfer Excited states Fluorophores Labeling Molecular oxygen Phosphorescence Proteins Spectroscopy Donor acceptors Excited state lifetimes Phosphorescence lifetime Photophysical properties Photophysics PLIM Pt complexes Reactive oxygen species Platinum compounds |
| description |
The synthesis and photophysical properties of a tailored Pt(II) complex are presented. The phosphorescence of its monomeric species in homogeneous solutions is quenched by interaction with the solvent and therefore absent even upon deoxygenation. However, aggregation-induced shielding from the environment and suppression of rotovibrational degrees of freedom trigger a phosphorescence turn-on that is not suppressed by molecular oxygen, despite possessing an excited-state lifetime ranging in the microsecond scale. Thus, the photoinduced production of reactive oxygen species is avoided by the suppression of diffusion-controlled Dexter-type energy transfer to triplet molecular oxygen. These aggregates emit with the characteristic green luminescence profile of monomeric complexes, indicating that Pt-Pt or excimeric interactions are negligible. Herein, we show that these aggregates can be used to label a model biomolecule (bovine serum albumin) with a microsecond-range luminescence. The protein stabilizes the aggregates, acting as a carrier in aqueous environments. Despite spectral overlaps, the green phosphorescence can be separated by time-gated detection from the dominant autofluorescence of the protein arising from a covalently bound green fluorophore that emits in the nanosecond range. Interestingly, the aggregates also acted as energy donors able to sensitize the emission of a fraction of the fluorophores bound to the protein. This resulted in a microsecond-range luminescence of the fluorescent acceptors and a shortening of the excited-state lifetime of the phosphorescent aggregates. The process that can be traced by a 1000-fold increase in the acceptor's lifetime mirrors the donor's triplet character. The implications for phosphorescence lifetime imaging are discussed. © 2018 American Chemical Society. |
| title |
Oxygen-Insensitive Aggregates of Pt(II) Complexes as Phosphorescent Labels of Proteins with Luminescence Lifetime-Based Readouts |
| title_short |
Oxygen-Insensitive Aggregates of Pt(II) Complexes as Phosphorescent Labels of Proteins with Luminescence Lifetime-Based Readouts |
| title_full |
Oxygen-Insensitive Aggregates of Pt(II) Complexes as Phosphorescent Labels of Proteins with Luminescence Lifetime-Based Readouts |
| title_fullStr |
Oxygen-Insensitive Aggregates of Pt(II) Complexes as Phosphorescent Labels of Proteins with Luminescence Lifetime-Based Readouts |
| title_full_unstemmed |
Oxygen-Insensitive Aggregates of Pt(II) Complexes as Phosphorescent Labels of Proteins with Luminescence Lifetime-Based Readouts |
| title_sort |
oxygen-insensitive aggregates of pt(ii) complexes as phosphorescent labels of proteins with luminescence lifetime-based readouts |
| publishDate |
2018 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19448244_v10_n29_p24361_Delcanale http://hdl.handle.net/20.500.12110/paper_19448244_v10_n29_p24361_Delcanale |
| _version_ |
1768543967296618496 |