Early aggregation steps in alpha-synuclein as measured by FCS and FRET: evidence for a contagious conformational change.

ABSTRACT: The kinetics of aggregation of alpha-synuclein are usually studied by turbidity or Thio-T fluorescence. Here we follow the disappearance of monomers and the formation of early oligomers using fluorescence correlation spectroscopy. Alexa488-labeled A140C-synuclein was used as a fluorescent probe in trace amounts in the presence of excess unlabeled alpha-synuclein. Repeated short measurements produce a distribution of diffusion coefficients. Initially, a sharp peak is obtained corresponding to monomers, followed by a distinct transient population and the gradual formation of broader-sized distributions of higher oligomers. The kinetics of aggregation can be followed by the decreasing number of fast-diffusing species. Both the disappearance of fast-diffusing species and the appearance of turb

SUBMITTER: Nath S 

PROVIDER: S-EPMC2849099 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature