Protein fibrillogenesis model tracked by its intrinsic time-resolved emission spectra

Li Hung C Chung, David J S Birch, Vladislav Vyshemirsky, Angelo Bella, Maxim G Ryadnov, Olaf J Rolinski

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

The excited-state kinetics of the fluorescence of tyrosine in a de novo protein fibrillogenesis model was investigated as a potential tool for monitoring protein fibre formation and complexation with glucose (glycation). In stark contrast to insulin the time-resolved emission spectra (TRES) recorded over the period of 700 hours in buffered solutions of the model with and without glucose revealed no apparent changes in Tyr fluorescence responses. This indicates the stability of the model and provides a measurement-supported basis for its use as a reference material in fluorescence studies of protein aggregation.

LanguageEnglish
Article number035003
Number of pages8
JournalMethods and Applications in Fluorescence
Volume7
Issue number3
DOIs
Publication statusPublished - 16 May 2019

Fingerprint

emission spectra
Fluorescence
proteins
Proteins
glucose
fluorescence
Glucose
insulin
tyrosine
Insulin
Complexation
Excited states
Tyrosine
Agglomeration
Kinetics
fibers
Fibers
Monitoring
kinetics
excitation

Keywords

  • protein fibrillogenesis
  • fluorescence intensity decay
  • time-resolved emission spectra
  • glycation

Cite this

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title = "Protein fibrillogenesis model tracked by its intrinsic time-resolved emission spectra",
abstract = "The excited-state kinetics of the fluorescence of tyrosine in a de novo protein fibrillogenesis model was investigated as a potential tool for monitoring protein fibre formation and complexation with glucose (glycation). In stark contrast to insulin the time-resolved emission spectra (TRES) recorded over the period of 700 hours in buffered solutions of the model with and without glucose revealed no apparent changes in Tyr fluorescence responses. This indicates the stability of the model and provides a measurement-supported basis for its use as a reference material in fluorescence studies of protein aggregation.",
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Protein fibrillogenesis model tracked by its intrinsic time-resolved emission spectra. / Chung, Li Hung C; Birch, David J S; Vyshemirsky, Vladislav; Bella, Angelo; Ryadnov, Maxim G; Rolinski, Olaf J.

In: Methods and Applications in Fluorescence , Vol. 7, No. 3, 035003, 16.05.2019.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Protein fibrillogenesis model tracked by its intrinsic time-resolved emission spectra

AU - Chung, Li Hung C

AU - Birch, David J S

AU - Vyshemirsky, Vladislav

AU - Bella, Angelo

AU - Ryadnov, Maxim G

AU - Rolinski, Olaf J

PY - 2019/5/16

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AB - The excited-state kinetics of the fluorescence of tyrosine in a de novo protein fibrillogenesis model was investigated as a potential tool for monitoring protein fibre formation and complexation with glucose (glycation). In stark contrast to insulin the time-resolved emission spectra (TRES) recorded over the period of 700 hours in buffered solutions of the model with and without glucose revealed no apparent changes in Tyr fluorescence responses. This indicates the stability of the model and provides a measurement-supported basis for its use as a reference material in fluorescence studies of protein aggregation.

KW - protein fibrillogenesis

KW - fluorescence intensity decay

KW - time-resolved emission spectra

KW - glycation

UR - https://iopscience.iop.org/journal/2050-6120

U2 - 10.1088/2050-6120/ab1985

DO - 10.1088/2050-6120/ab1985

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VL - 7

JO - Methods and Applications in Fluorescence

T2 - Methods and Applications in Fluorescence

JF - Methods and Applications in Fluorescence

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