Amyloids are insoluble fibrous protein aggregates that have been associated with the pathology of a range of human diseases, most notably Alzheimer’s Disease (AD). Beyond AD, diseases associated with the formation of amyloid deposits include Parkinson’s Disease, Spongiform encephalopathy (more commonly referred to as mad cow disease), and a range of dementias and prion diseases. Other neurodegenerative diseases, including Huntingdon’s Disease (HD) and Amyotrophic lateral sclerosis (ALS), are associated with the pathological aggregation of specific amyloidogenic proteins. Altogether more than forty of these “protein deposition” diseases have been described so far, making this at once one of the most important, but also one of the more intractable, problems in biomedicine.
While no efficacious treatments have yet been found to delay or stop the progression of AD, remarkable scientific advances continue to be made in our understanding of these various pathologies. More importantly a unified picture of the molecular and clinical features of protein misfolding and aggregation is emerging, yielding the exciting prospect of therapeutic advances that might be applicable across more than one disease.
This symposium will highlight some of the key advances made to date in our understanding of the molecular characteristics underpinning these clinical pathologies. Key biochemical targets will be highlighted, along with the challenges that these pose to the development of therapeutics.

About the Brother Lucian Blersch Symposium

Organized by the School of Natural Sciences at St. Edward’s University, the event is free and open to the public. This symposium honors Brother Lucian Blersch, CSC, a longtime professor of Engineering at St. Edward’s who died in 1986 and in whose name a professorship in the School of Natural Sciences was endowed by a gift from J.B.N. Morris hs ’48, ’52, and his family.

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