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World class computing and information science research at Strathclyde...

The Strathprints institutional repository is a digital archive of University of Strathclyde's Open Access research outputs. Strathprints provides access to thousands of Open Access research papers by University of Strathclyde researchers, including by researchers from the Department of Computer & Information Sciences involved in mathematically structured programming, similarity and metric search, computer security, software systems, combinatronics and digital health.

The Department also includes the iSchool Research Group, which performs leading research into socio-technical phenomena and topics such as information retrieval and information seeking behaviour.

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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