Tyrosine photophysics during the early stages of β-amyloid aggregation leading to Alzheimer's

Olaf J. Rolinski, Thorben Wellbrock, David J. S. Birch, Vladislav Vyshemirsky

Research output: Contribution to journalLetter

7 Citations (Scopus)

Abstract

We have monitored the formation of toxic β-amyloid oligomers leading to Alzheimer's disease by detecting changes in the fluorescence decay of intrinsic tyrosine. A new approach based on the non-Debye model of fluorescence kinetics resolves the complexity of the underlying photophysics. The gradual disappearance of nonmonotonic fluorescence decay rates, at the early stages of aggregation as larger, tighter-packed oligomers are formed, is interpreted in terms of tyrosine-peptide dielectric relaxation influencing the decay. The results demonstrate the potential for a new type of fluorescence lifetime sensing based on dual excited-state/dielectric relaxation, with application across a broad range of biological molecules. The results also reconcile previously conflicting models of protein intrinsic fluorescence decay based on rotamers or dielectric relaxation by illustrating conditions under which both are manifest.

LanguageEnglish
Pages3116-3120
Number of pages5
JournalJournal of Physical Chemistry Letters
Volume6
Issue number15
DOIs
Publication statusPublished - 28 Jul 2015

Fingerprint

tyrosine
Amyloid
Tyrosine
Agglomeration
Fluorescence
Dielectric relaxation
fluorescence
oligomers
Oligomers
decay
Poisons
Excited states
Peptides
decay rates
peptides
proteins
Proteins
life (durability)
Molecules
Kinetics

Keywords

  • Alzheimer's disease
  • non-Debye kinetics
  • protein fluorescence
  • tyrosine
  • β-amyloid aggregation

Cite this

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abstract = "We have monitored the formation of toxic β-amyloid oligomers leading to Alzheimer's disease by detecting changes in the fluorescence decay of intrinsic tyrosine. A new approach based on the non-Debye model of fluorescence kinetics resolves the complexity of the underlying photophysics. The gradual disappearance of nonmonotonic fluorescence decay rates, at the early stages of aggregation as larger, tighter-packed oligomers are formed, is interpreted in terms of tyrosine-peptide dielectric relaxation influencing the decay. The results demonstrate the potential for a new type of fluorescence lifetime sensing based on dual excited-state/dielectric relaxation, with application across a broad range of biological molecules. The results also reconcile previously conflicting models of protein intrinsic fluorescence decay based on rotamers or dielectric relaxation by illustrating conditions under which both are manifest.",
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Tyrosine photophysics during the early stages of β-amyloid aggregation leading to Alzheimer's. / Rolinski, Olaf J.; Wellbrock, Thorben; Birch, David J. S.; Vyshemirsky, Vladislav.

In: Journal of Physical Chemistry Letters, Vol. 6, No. 15, 28.07.2015, p. 3116-3120.

Research output: Contribution to journalLetter

TY - JOUR

T1 - Tyrosine photophysics during the early stages of β-amyloid aggregation leading to Alzheimer's

AU - Rolinski, Olaf J.

AU - Wellbrock, Thorben

AU - Birch, David J. S.

AU - Vyshemirsky, Vladislav

PY - 2015/7/28

Y1 - 2015/7/28

N2 - We have monitored the formation of toxic β-amyloid oligomers leading to Alzheimer's disease by detecting changes in the fluorescence decay of intrinsic tyrosine. A new approach based on the non-Debye model of fluorescence kinetics resolves the complexity of the underlying photophysics. The gradual disappearance of nonmonotonic fluorescence decay rates, at the early stages of aggregation as larger, tighter-packed oligomers are formed, is interpreted in terms of tyrosine-peptide dielectric relaxation influencing the decay. The results demonstrate the potential for a new type of fluorescence lifetime sensing based on dual excited-state/dielectric relaxation, with application across a broad range of biological molecules. The results also reconcile previously conflicting models of protein intrinsic fluorescence decay based on rotamers or dielectric relaxation by illustrating conditions under which both are manifest.

AB - We have monitored the formation of toxic β-amyloid oligomers leading to Alzheimer's disease by detecting changes in the fluorescence decay of intrinsic tyrosine. A new approach based on the non-Debye model of fluorescence kinetics resolves the complexity of the underlying photophysics. The gradual disappearance of nonmonotonic fluorescence decay rates, at the early stages of aggregation as larger, tighter-packed oligomers are formed, is interpreted in terms of tyrosine-peptide dielectric relaxation influencing the decay. The results demonstrate the potential for a new type of fluorescence lifetime sensing based on dual excited-state/dielectric relaxation, with application across a broad range of biological molecules. The results also reconcile previously conflicting models of protein intrinsic fluorescence decay based on rotamers or dielectric relaxation by illustrating conditions under which both are manifest.

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KW - non-Debye kinetics

KW - protein fluorescence

KW - tyrosine

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JO - Journal of Physical Chemistry Letters

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