Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity
oleh: Amberley D. Stephens, Maria Zacharopoulou, Rani Moons, Giuliana Fusco, Neeleema Seetaloo, Anass Chiki, Philippa J. Woodhams, Ioanna Mela, Hilal A. Lashuel, Jonathan J. Phillips, Alfonso De Simone, Frank Sobott, Gabriele S. Kaminski Schierle
| Format: | Article |
|---|---|
| Diterbitkan: | Nature Portfolio 2020-06-01 |
Deskripsi
In Parkinson’s disease (PD) the monomeric protein alpha-synuclein (aSyn) misfolds and aggregates into insoluble fibrils. Here the authors use NMR measurements and hydrogen–deuterium exchange mass spectrometry and find that the more solvent exposed the N-terminus of aSyn is, the more aggregation prone its conformation becomes, and further show how PD mutations and post translational modifications influence the extent of the N-terminus solvent exposure.