Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein.

KIM, HY, HEINSE, Y, FERNANDEZ, CO, BALDUS M, ZWECKSTETER, M.

CHEMBIOCHEM

Año: 2007 vol. 8 p. 1671 - 1674

1439-4227

Many neurodegenerative disorders are associated with the deposition of amyloid fibrils. Aggregation is generally initiated by unfolding of the native state of the aggregating protein, then conversion into beta-sheet rich architecture. Using solution and solid-state NMR spectroscopy, we show that the secondary structure of alpha-synuclein fibrils, the major component of deposits in Parkinson disease, correlates directly with the structural properties of the unfolded sate.