Direct characterization of amyloidogenic oligomers by single-molecule fluorescence.

ABSTRACT: A key issue in understanding the pathogenic conditions associated with the aberrant aggregation of misfolded proteins is the identification and characterization of species formed during the aggregation process. Probing the nature of such species has, however, proved to be extremely challenging to conventional techniques because of their transient and heterogeneous character. We describe here the application of a two-color single-molecule fluorescence technique to examine the assembly of oligomeric species formed during the aggregation of the SH3 domain of PI3 kinase. The single-molecule experiments show that the species formed at the stage of the reaction where aggregates have previously been found to be maximally cytotoxic are a heterogeneous ensemble of oligomers with a median size of 38

SUBMITTER: Orte A 

PROVIDER: S-EPMC2567173 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature