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Compact Conformations of α-Synuclein Induced by Alcohols and Copper by Antonino Natalello; Federico Benetti; Silvia Maria Doglia; Giuseppe Legname; Rita Grandori is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract The intrinsically disordered protein α‐synuclein aggregates into amyloid fibrils, a process known to be implicated in several neurodegenerative states. Partially folded forms of the protein are thought to trigger the aggregation process. Here, α‐synuclein conformers are characterized by analysis of the charge‐state distributions observed in electrospray‐ionization mass spectrometry under negative‐ion mode. It is found that, even at neutral pH, a small fraction of the molecular population is in a compact conformation. Several distinct partially folded forms are then identified under conditions that promote α‐synuclein aggregation, such as solutions of simple and fluorinated alcohols. Specific intermediates accumulate at increasing concentrations of ethanol, hexafluoro‐2‐propanol, and trifluoroethanol. Finally, extensive folding induced by Cu^2+^ binding is revealed by titrations in the presence of Cu^2+^–glycine. The data confirm the existence of a single, high‐affinity binding site for Cu^2+^. Because accumulation of this partially folded form correlates with enhancement of fibrillation kinetics, it is likely to represent an amyloidogenic intermediate in α‐synuclein con

Who reads Compact Conformations of α-Synuclein Induced by Alcohols and Copper?

Author

Antonino Natalello; Federico Benetti; Silvia Maria Doglia; Giuseppe Legname; Rita Grandori

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

2010

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)