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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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. ![]() ![]() | Item type: | Article |
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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: | 20 Jan 2021 19:20 |
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URI: | https://strathprints.strath.ac.uk/id/eprint/31130 |
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