Beta-amyloid oligomerisation monitored by intrinsic tyrosine fluorescence

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

Aggregation of the peptide beta-amyloid is known to be associated with Alzheimer's disease. According to recent findings the most neurotoxic aggregates are the oligomers formed in the initial stages of the aggregation process. Here we use beta-amyloid's (A beta's) intrinsic fluorophore tyrosine to probe the earliest peptide-to-peptide stages of aggregation, a region often merely labelled as a time lag, because negligible changes are observed by the commonly used probe ThT. Using spectrally resolved fluorescence decay time techniques and analysis we demonstrate how the distribution of 3 rotamer conformations of the single tyrosine in A beta tracks the aggregation across the time lag and beyond according to the initial peptide concentration. At low A beta concentrations
LanguageEnglish
Pages6434-6441
Number of pages8
JournalPhysical Chemistry Chemical Physics
Volume13
Issue number14
DOIs
Publication statusPublished - 4 Mar 2011

Fingerprint

Oligomerization
tyrosine
Amyloid
peptides
Tyrosine
Agglomeration
Fluorescence
fluorescence
Peptides
time lag
Fluorophores
probes
Amyloid beta-Peptides
oligomers
Oligomers
Conformations
decay

Keywords

  • protein aggregation
  • fibrils
  • peptides
  • conversion
  • fibrillation
  • Thioflavin-T
  • alpha-synuclein

Cite this

@article{b943b3b45f6c4ba5aee4e2435ad82456,
title = "Beta-amyloid oligomerisation monitored by intrinsic tyrosine fluorescence",
abstract = "Aggregation of the peptide beta-amyloid is known to be associated with Alzheimer's disease. According to recent findings the most neurotoxic aggregates are the oligomers formed in the initial stages of the aggregation process. Here we use beta-amyloid's (A beta's) intrinsic fluorophore tyrosine to probe the earliest peptide-to-peptide stages of aggregation, a region often merely labelled as a time lag, because negligible changes are observed by the commonly used probe ThT. Using spectrally resolved fluorescence decay time techniques and analysis we demonstrate how the distribution of 3 rotamer conformations of the single tyrosine in A beta tracks the aggregation across the time lag and beyond according to the initial peptide concentration. At low A beta concentrations",
keywords = "protein aggregation , fibrils, peptides, conversion, fibrillation, Thioflavin-T, alpha-synuclein",
author = "Mariana Amaro and Birch, {David J. S.} and Rolinski, {Olaf J.}",
year = "2011",
month = "3",
day = "4",
doi = "10.1039/c0cp02652b",
language = "English",
volume = "13",
pages = "6434--6441",
journal = "Physical Chemistry Chemical Physics",
issn = "1463-9076",
number = "14",

}

Beta-amyloid oligomerisation monitored by intrinsic tyrosine fluorescence. / Amaro, Mariana; Birch, David J. S.; Rolinski, Olaf J.

In: Physical Chemistry Chemical Physics, Vol. 13, No. 14, 04.03.2011, p. 6434-6441.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Beta-amyloid oligomerisation monitored by intrinsic tyrosine fluorescence

AU - Amaro, Mariana

AU - Birch, David J. S.

AU - Rolinski, Olaf J.

PY - 2011/3/4

Y1 - 2011/3/4

N2 - Aggregation of the peptide beta-amyloid is known to be associated with Alzheimer's disease. According to recent findings the most neurotoxic aggregates are the oligomers formed in the initial stages of the aggregation process. Here we use beta-amyloid's (A beta's) intrinsic fluorophore tyrosine to probe the earliest peptide-to-peptide stages of aggregation, a region often merely labelled as a time lag, because negligible changes are observed by the commonly used probe ThT. Using spectrally resolved fluorescence decay time techniques and analysis we demonstrate how the distribution of 3 rotamer conformations of the single tyrosine in A beta tracks the aggregation across the time lag and beyond according to the initial peptide concentration. At low A beta concentrations

AB - Aggregation of the peptide beta-amyloid is known to be associated with Alzheimer's disease. According to recent findings the most neurotoxic aggregates are the oligomers formed in the initial stages of the aggregation process. Here we use beta-amyloid's (A beta's) intrinsic fluorophore tyrosine to probe the earliest peptide-to-peptide stages of aggregation, a region often merely labelled as a time lag, because negligible changes are observed by the commonly used probe ThT. Using spectrally resolved fluorescence decay time techniques and analysis we demonstrate how the distribution of 3 rotamer conformations of the single tyrosine in A beta tracks the aggregation across the time lag and beyond according to the initial peptide concentration. At low A beta concentrations

KW - protein aggregation

KW - fibrils

KW - peptides

KW - conversion

KW - fibrillation

KW - Thioflavin-T

KW - alpha-synuclein

UR - http://www.scopus.com/inward/record.url?scp=79952913247&partnerID=8YFLogxK

U2 - 10.1039/c0cp02652b

DO - 10.1039/c0cp02652b

M3 - Article

VL - 13

SP - 6434

EP - 6441

JO - Physical Chemistry Chemical Physics

T2 - Physical Chemistry Chemical Physics

JF - Physical Chemistry Chemical Physics

SN - 1463-9076

IS - 14

ER -