Pathogenic mutations shift the equilibria of alpha-synuclein single molecules towards structured conformers.

@article{Brucale2009PathogenicMS,
  title={Pathogenic mutations shift the equilibria of alpha-synuclein single molecules towards structured conformers.},
  author={Marco Brucale and Massimo Sandal and Selena Di Maio and Aldo Rampioni and Isabella Tessari and Laura Tosatto and Marco Bisaglia and Luigi Bubacco and Bruno Samor{\`i}},
  journal={Chembiochem : a European journal of chemical biology},
  year={2009},
  volume={10 1},
  pages={176-83}
}
Alpha-synuclein (alpha-Syn) is an abundant brain protein whose mutations have been linked to early-onset Parkinson's disease (PD). We recently demonstrated, by means of a single-molecule force spectroscopy (SMFS) methodology, that the conformational equilibrium of monomeric wild-type (WT) alpha-Syn shifts toward beta-containing structures in several unrelated conditions linked to PD pathogenicity. Herein, we follow the same methodology previously employed for WT alpha-Syn to characterize the… CONTINUE READING