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The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs.

Strathprints serves world leading Open Access research by the University of Strathclyde, including research by the Strathclyde Institute of Pharmacy and Biomedical Sciences (SIPBS), where research centres such as the Industrial Biotechnology Innovation Centre (IBioIC), the Cancer Research UK Formulation Unit, SeaBioTech and the Centre for Biophotonics are based.

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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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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