<i>In vitro</i>-prepared A30P alpha-synuclein fibrils adopt the conserved and disease-relevant Greek key fold.

ABSTRACT: The pathological hallmark of Parkinson Disease (PD) is the formation of the protein alpha-synuclein (Asyn) into β-sheet rich, self-templating fibrils in the brain. Since the first atomic structure of wild-type Asyn fibrils was determined nearly a decade ago, several other in vitro structures of hereditary mutant fibrils and structures derived from post-mortem diseased patient tissue have been determined by solid-state nuclear magnetic resonance (SSNMR) spectroscopy and cryo-electron microscopy. These structures have not only expanded the library of structures available for computational modeling of drug binding and therapeutics development but have also given unprecedented insight into the disease specificity and structural polymorphism of Asyn fibrils. Here, we report the high-reso

SUBMITTER: Milchberg MH 

PROVIDER: S-EPMC12889639 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature