The major pathological hallmark of Alzheimer's disease is the accumulation of �-amyloid (A�) peptide within amyloid plaques in the brain.  When forming the cross-� structure typical of amyloid fibrils, there is some inherent flexibility regarding the intermolecular contacts that the A� peptide can adopt.  As a result, the fibril structure may vary, resulting in distinct conformational strains.  While a specific primary sequence is able to adopt multiple strain conformations, it is not known how disease-associated mutations occurring within that sequence may alter the fibril structure.  We are using biophysical methods to determine whether certain A� mutants form unique fibril strains that propagate their particular structure irrespective of primary sequence.

Examining disease-associated A� mutants as conformational strains

248th National Meeting (2014)

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