Fluorescence Investigation of Interactions Between Novel Benzanthrone Dyes and Lysozyme Amyloid Fibrils
Abstract A series of novel fluorescent benzanthrone dyes have been tested for their ability to identify and characterize fibrillar aggregates of lysozyme prepared by protein denaturation in concentrated ethanol solution ($ F_{eth} $) or acidic buffer ($ F_{ac} $). Quantitative parameters of the dye...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Vus, Kateryna [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2013 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer Science+Business Media New York 2013 |
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| Übergeordnetes Werk: |
Enthalten in: Journal of fluorescence - Springer US, 1991, 24(2013), 2 vom: 27. Dez., Seite 493-504 |
|---|---|
| Übergeordnetes Werk: |
volume:24 ; year:2013 ; number:2 ; day:27 ; month:12 ; pages:493-504 |
| Links: |
|---|
| DOI / URN: |
10.1007/s10895-013-1318-3 |
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OLC2070054322 |
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| 520 | |a Abstract A series of novel fluorescent benzanthrone dyes have been tested for their ability to identify and characterize fibrillar aggregates of lysozyme prepared by protein denaturation in concentrated ethanol solution ($ F_{eth} $) or acidic buffer ($ F_{ac} $). Quantitative parameters of the dye association with native and fibrillar protein have been derived from the results of fluorimetric titration. The binding characteristics proved to be different for $ F_{eth} $- and $ F_{ac} $-bound benzanthrones, highlighting the dye sensitivity to the distinctions in fibril morphology. By comparing the dye preference to fibrillar protein aggregates, AM2, A8 and A6 were selected as the most prospective amyloid tracers. Based on the analysis of red edge excitation shifts and fluorescence lifetimes of the amyloid-bound dyes it was assumed that surface grooves or dry “steric zipper” interface are potential fibril binding sites for the novel fluorophores. | ||
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| 700 | 1 | |a Kinnunen, Paavo |4 aut | |
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10.1007/s10895-013-1318-3 doi (DE-627)OLC2070054322 (DE-He213)s10895-013-1318-3-p DE-627 ger DE-627 rakwb eng 620 VZ Vus, Kateryna verfasserin aut Fluorescence Investigation of Interactions Between Novel Benzanthrone Dyes and Lysozyme Amyloid Fibrils 2013 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media New York 2013 Abstract A series of novel fluorescent benzanthrone dyes have been tested for their ability to identify and characterize fibrillar aggregates of lysozyme prepared by protein denaturation in concentrated ethanol solution ($ F_{eth} $) or acidic buffer ($ F_{ac} $). Quantitative parameters of the dye association with native and fibrillar protein have been derived from the results of fluorimetric titration. The binding characteristics proved to be different for $ F_{eth} $- and $ F_{ac} $-bound benzanthrones, highlighting the dye sensitivity to the distinctions in fibril morphology. By comparing the dye preference to fibrillar protein aggregates, AM2, A8 and A6 were selected as the most prospective amyloid tracers. Based on the analysis of red edge excitation shifts and fluorescence lifetimes of the amyloid-bound dyes it was assumed that surface grooves or dry “steric zipper” interface are potential fibril binding sites for the novel fluorophores. Benzanthrone dyes Amyloid marker Fibrillar lysozyme Polarity Trusova, Valeriya aut Gorbenko, Galyna aut Sood, Rohit aut Kirilova, Elena aut Kirilov, Georgiy aut Kalnina, Inta aut Kinnunen, Paavo aut Enthalten in Journal of fluorescence Springer US, 1991 24(2013), 2 vom: 27. Dez., Seite 493-504 (DE-627)130988731 (DE-600)1079500-5 (DE-576)030293898 1053-0509 nnns volume:24 year:2013 number:2 day:27 month:12 pages:493-504 https://doi.org/10.1007/s10895-013-1318-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 AR 24 2013 2 27 12 493-504 |
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10.1007/s10895-013-1318-3 doi (DE-627)OLC2070054322 (DE-He213)s10895-013-1318-3-p DE-627 ger DE-627 rakwb eng 620 VZ Vus, Kateryna verfasserin aut Fluorescence Investigation of Interactions Between Novel Benzanthrone Dyes and Lysozyme Amyloid Fibrils 2013 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media New York 2013 Abstract A series of novel fluorescent benzanthrone dyes have been tested for their ability to identify and characterize fibrillar aggregates of lysozyme prepared by protein denaturation in concentrated ethanol solution ($ F_{eth} $) or acidic buffer ($ F_{ac} $). Quantitative parameters of the dye association with native and fibrillar protein have been derived from the results of fluorimetric titration. The binding characteristics proved to be different for $ F_{eth} $- and $ F_{ac} $-bound benzanthrones, highlighting the dye sensitivity to the distinctions in fibril morphology. By comparing the dye preference to fibrillar protein aggregates, AM2, A8 and A6 were selected as the most prospective amyloid tracers. Based on the analysis of red edge excitation shifts and fluorescence lifetimes of the amyloid-bound dyes it was assumed that surface grooves or dry “steric zipper” interface are potential fibril binding sites for the novel fluorophores. Benzanthrone dyes Amyloid marker Fibrillar lysozyme Polarity Trusova, Valeriya aut Gorbenko, Galyna aut Sood, Rohit aut Kirilova, Elena aut Kirilov, Georgiy aut Kalnina, Inta aut Kinnunen, Paavo aut Enthalten in Journal of fluorescence Springer US, 1991 24(2013), 2 vom: 27. Dez., Seite 493-504 (DE-627)130988731 (DE-600)1079500-5 (DE-576)030293898 1053-0509 nnns volume:24 year:2013 number:2 day:27 month:12 pages:493-504 https://doi.org/10.1007/s10895-013-1318-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 AR 24 2013 2 27 12 493-504 |
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10.1007/s10895-013-1318-3 doi (DE-627)OLC2070054322 (DE-He213)s10895-013-1318-3-p DE-627 ger DE-627 rakwb eng 620 VZ Vus, Kateryna verfasserin aut Fluorescence Investigation of Interactions Between Novel Benzanthrone Dyes and Lysozyme Amyloid Fibrils 2013 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media New York 2013 Abstract A series of novel fluorescent benzanthrone dyes have been tested for their ability to identify and characterize fibrillar aggregates of lysozyme prepared by protein denaturation in concentrated ethanol solution ($ F_{eth} $) or acidic buffer ($ F_{ac} $). Quantitative parameters of the dye association with native and fibrillar protein have been derived from the results of fluorimetric titration. The binding characteristics proved to be different for $ F_{eth} $- and $ F_{ac} $-bound benzanthrones, highlighting the dye sensitivity to the distinctions in fibril morphology. By comparing the dye preference to fibrillar protein aggregates, AM2, A8 and A6 were selected as the most prospective amyloid tracers. Based on the analysis of red edge excitation shifts and fluorescence lifetimes of the amyloid-bound dyes it was assumed that surface grooves or dry “steric zipper” interface are potential fibril binding sites for the novel fluorophores. Benzanthrone dyes Amyloid marker Fibrillar lysozyme Polarity Trusova, Valeriya aut Gorbenko, Galyna aut Sood, Rohit aut Kirilova, Elena aut Kirilov, Georgiy aut Kalnina, Inta aut Kinnunen, Paavo aut Enthalten in Journal of fluorescence Springer US, 1991 24(2013), 2 vom: 27. Dez., Seite 493-504 (DE-627)130988731 (DE-600)1079500-5 (DE-576)030293898 1053-0509 nnns volume:24 year:2013 number:2 day:27 month:12 pages:493-504 https://doi.org/10.1007/s10895-013-1318-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 AR 24 2013 2 27 12 493-504 |
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10.1007/s10895-013-1318-3 doi (DE-627)OLC2070054322 (DE-He213)s10895-013-1318-3-p DE-627 ger DE-627 rakwb eng 620 VZ Vus, Kateryna verfasserin aut Fluorescence Investigation of Interactions Between Novel Benzanthrone Dyes and Lysozyme Amyloid Fibrils 2013 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media New York 2013 Abstract A series of novel fluorescent benzanthrone dyes have been tested for their ability to identify and characterize fibrillar aggregates of lysozyme prepared by protein denaturation in concentrated ethanol solution ($ F_{eth} $) or acidic buffer ($ F_{ac} $). Quantitative parameters of the dye association with native and fibrillar protein have been derived from the results of fluorimetric titration. The binding characteristics proved to be different for $ F_{eth} $- and $ F_{ac} $-bound benzanthrones, highlighting the dye sensitivity to the distinctions in fibril morphology. By comparing the dye preference to fibrillar protein aggregates, AM2, A8 and A6 were selected as the most prospective amyloid tracers. Based on the analysis of red edge excitation shifts and fluorescence lifetimes of the amyloid-bound dyes it was assumed that surface grooves or dry “steric zipper” interface are potential fibril binding sites for the novel fluorophores. Benzanthrone dyes Amyloid marker Fibrillar lysozyme Polarity Trusova, Valeriya aut Gorbenko, Galyna aut Sood, Rohit aut Kirilova, Elena aut Kirilov, Georgiy aut Kalnina, Inta aut Kinnunen, Paavo aut Enthalten in Journal of fluorescence Springer US, 1991 24(2013), 2 vom: 27. Dez., Seite 493-504 (DE-627)130988731 (DE-600)1079500-5 (DE-576)030293898 1053-0509 nnns volume:24 year:2013 number:2 day:27 month:12 pages:493-504 https://doi.org/10.1007/s10895-013-1318-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 AR 24 2013 2 27 12 493-504 |
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10.1007/s10895-013-1318-3 doi (DE-627)OLC2070054322 (DE-He213)s10895-013-1318-3-p DE-627 ger DE-627 rakwb eng 620 VZ Vus, Kateryna verfasserin aut Fluorescence Investigation of Interactions Between Novel Benzanthrone Dyes and Lysozyme Amyloid Fibrils 2013 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media New York 2013 Abstract A series of novel fluorescent benzanthrone dyes have been tested for their ability to identify and characterize fibrillar aggregates of lysozyme prepared by protein denaturation in concentrated ethanol solution ($ F_{eth} $) or acidic buffer ($ F_{ac} $). Quantitative parameters of the dye association with native and fibrillar protein have been derived from the results of fluorimetric titration. The binding characteristics proved to be different for $ F_{eth} $- and $ F_{ac} $-bound benzanthrones, highlighting the dye sensitivity to the distinctions in fibril morphology. By comparing the dye preference to fibrillar protein aggregates, AM2, A8 and A6 were selected as the most prospective amyloid tracers. Based on the analysis of red edge excitation shifts and fluorescence lifetimes of the amyloid-bound dyes it was assumed that surface grooves or dry “steric zipper” interface are potential fibril binding sites for the novel fluorophores. Benzanthrone dyes Amyloid marker Fibrillar lysozyme Polarity Trusova, Valeriya aut Gorbenko, Galyna aut Sood, Rohit aut Kirilova, Elena aut Kirilov, Georgiy aut Kalnina, Inta aut Kinnunen, Paavo aut Enthalten in Journal of fluorescence Springer US, 1991 24(2013), 2 vom: 27. Dez., Seite 493-504 (DE-627)130988731 (DE-600)1079500-5 (DE-576)030293898 1053-0509 nnns volume:24 year:2013 number:2 day:27 month:12 pages:493-504 https://doi.org/10.1007/s10895-013-1318-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_70 AR 24 2013 2 27 12 493-504 |
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Fluorescence Investigation of Interactions Between Novel Benzanthrone Dyes and Lysozyme Amyloid Fibrils |
| abstract |
Abstract A series of novel fluorescent benzanthrone dyes have been tested for their ability to identify and characterize fibrillar aggregates of lysozyme prepared by protein denaturation in concentrated ethanol solution ($ F_{eth} $) or acidic buffer ($ F_{ac} $). Quantitative parameters of the dye association with native and fibrillar protein have been derived from the results of fluorimetric titration. The binding characteristics proved to be different for $ F_{eth} $- and $ F_{ac} $-bound benzanthrones, highlighting the dye sensitivity to the distinctions in fibril morphology. By comparing the dye preference to fibrillar protein aggregates, AM2, A8 and A6 were selected as the most prospective amyloid tracers. Based on the analysis of red edge excitation shifts and fluorescence lifetimes of the amyloid-bound dyes it was assumed that surface grooves or dry “steric zipper” interface are potential fibril binding sites for the novel fluorophores. © Springer Science+Business Media New York 2013 |
| abstractGer |
Abstract A series of novel fluorescent benzanthrone dyes have been tested for their ability to identify and characterize fibrillar aggregates of lysozyme prepared by protein denaturation in concentrated ethanol solution ($ F_{eth} $) or acidic buffer ($ F_{ac} $). Quantitative parameters of the dye association with native and fibrillar protein have been derived from the results of fluorimetric titration. The binding characteristics proved to be different for $ F_{eth} $- and $ F_{ac} $-bound benzanthrones, highlighting the dye sensitivity to the distinctions in fibril morphology. By comparing the dye preference to fibrillar protein aggregates, AM2, A8 and A6 were selected as the most prospective amyloid tracers. Based on the analysis of red edge excitation shifts and fluorescence lifetimes of the amyloid-bound dyes it was assumed that surface grooves or dry “steric zipper” interface are potential fibril binding sites for the novel fluorophores. © Springer Science+Business Media New York 2013 |
| abstract_unstemmed |
Abstract A series of novel fluorescent benzanthrone dyes have been tested for their ability to identify and characterize fibrillar aggregates of lysozyme prepared by protein denaturation in concentrated ethanol solution ($ F_{eth} $) or acidic buffer ($ F_{ac} $). Quantitative parameters of the dye association with native and fibrillar protein have been derived from the results of fluorimetric titration. The binding characteristics proved to be different for $ F_{eth} $- and $ F_{ac} $-bound benzanthrones, highlighting the dye sensitivity to the distinctions in fibril morphology. By comparing the dye preference to fibrillar protein aggregates, AM2, A8 and A6 were selected as the most prospective amyloid tracers. Based on the analysis of red edge excitation shifts and fluorescence lifetimes of the amyloid-bound dyes it was assumed that surface grooves or dry “steric zipper” interface are potential fibril binding sites for the novel fluorophores. © Springer Science+Business Media New York 2013 |
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| title_short |
Fluorescence Investigation of Interactions Between Novel Benzanthrone Dyes and Lysozyme Amyloid Fibrils |
| url |
https://doi.org/10.1007/s10895-013-1318-3 |
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| author2 |
Trusova, Valeriya Gorbenko, Galyna Sood, Rohit Kirilova, Elena Kirilov, Georgiy Kalnina, Inta Kinnunen, Paavo |
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Trusova, Valeriya Gorbenko, Galyna Sood, Rohit Kirilova, Elena Kirilov, Georgiy Kalnina, Inta Kinnunen, Paavo |
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130988731 |
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| doi_str |
10.1007/s10895-013-1318-3 |
| up_date |
2024-07-04T00:07:04.589Z |
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