Beta-amyloid oligomerisation monitored by intrinsic tyrosine fluorescence

Amaro, Mariana and Birch, David J. S. and Rolinski, Olaf J. (2011) Beta-amyloid oligomerisation monitored by intrinsic tyrosine fluorescence. Physical Chemistry Chemical Physics, 13 (14). pp. 6434-6441. ISSN 1463-9076

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Official URL: https://doi.org/10.1039/c0cp02652b

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

Creators(s):	Amaro, Mariana, Birch, David J. S. ORCID: https://orcid.org/0000-0001-6400-1270 and Rolinski, Olaf J. ORCID: https://orcid.org/0000-0002-7838-779X;
Item type:	Article
ID code:	31130
Keywords:	protein aggregation , fibrils, peptides, conversion, fibrillation, Thioflavin-T, alpha-synuclein, Physics, Chemistry, Physics and Astronomy(all), Physical and Theoretical Chemistry
Subjects:	Science > Physics Science > Chemistry
Department:	Faculty of Science > Physics Technology and Innovation Centre > Bionanotechnology
Depositing user:	Pure Administrator
Date deposited:	17 May 2011 11:01
Last modified:	13 Aug 2020 03:03
Related URLs:	Scopus publication
URI:	https://strathprints.strath.ac.uk/id/eprint/31130
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