Oligomer Diversity during the Aggregation of the Repeat Region of Tau.

ABSTRACT: The molecular mechanism of protein aggregation is of both fundamental and clinical importance as amyloid aggregates are linked to a number of neurodegenerative disorders. Such protein aggregates include macroscopic insoluble fibrils as well as small soluble oligomeric species. Time-dependent resolution of these species is prerequisite for a detailed quantitative understanding of protein aggregation; this remains challenging due to the lack of methods for detecting and characterizing transient and heterogeneous protein oligomers. Here we have used single molecule fluorescence techniques combined with mechanistic modeling to study the heparin-induced aggregation of the repeat region of tau, which forms the core region of neurofibrillary tangles found in Alzheimer's disease. We distinguish se

SUBMITTER: Kjaergaard M 

PROVIDER: S-EPMC6302314 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature