As life expectancy rises certain diseases are becoming more abundant. Alzheimer’s is one such example for which there is no clinical diagnosis and no cure. The formation of fibrils and plaques in the brain that are composed of peptides is a symptom of Alzheimer’s, but it is now widely accepted that it is the early oligomers (aggregates) of the peptide beta-amyloid that are thought to be the cytotoxic agents. Not only is there no non-invasive technique available for detecting the disease in its early stages, but research into finding new therapeutics has been hampered by an inability to detect the early stage of oligomerization of beta-amyloid in vitro.
The Strathclyde Photophysics team have recently made great strides in overcoming this barrier to progress by monitoring the oligomerization of beta-amyloid by means of the intrinsic fluorescence of the amino acid tyrosine that occurs naturally in beta-amyloid.
· Improved method for assessing intervention therapies for Alzheimer’s disease
· Monitoring the effect of initiators and accelerants in respect of Alzheimer’s disease
· The findings for Alzheimer’s are likely to have bearing on other neurodegenerative diseases
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Alzheimer’s afflicts 5% of men and 6 % of women over 60 with greater than 60m afflicted at present and greater than 100m predicted by 2050. The research also has wider bearing on other neurological diseases and beyond e.g. Parkinson’s and Huntingtons’ diseases follow a similar process with other protein, as do cataracts in the eye. The mechanism of protein aggregation to form fibrils is a general phenomena that once better understood could also pave the way to the fabrication of new materials.
We would be interested in collaborative research with pharmaceutical companies with a view to reducing their lead times for drug discovery using our approach.