Data supporting the publication "Unravelling the Structure and Dynamics of Ac-PHF6-NH2 Tau Segment Oligomers"
This repository contains raw data that were used to draw conclusions and generate figures for the paper "Unravelling the Structure and Dynamics of Ac-PHF6-NH2 Tau Segment Oligomers". It includes readme files, raw data, and processed data. In this paper, we have employed a combined approach that allows us to probe the structure and kinetics of the emergence of oligomeric species, following them over time as they form fibrillar structures. Targeting the tau protein peptide seg-ment Ac-PHF6-NH2, which is crucial for the aggregation of the full protein, soft nano-electrospray ionization combined with ion mobility mass spectrometry has been employed to study the kinetics of heparin-induced intact oligomer formation. The formed oligomers are identified and characterized using high-resolution ion mobility mass spectrometry, demonstrating that the addition of heparin does not alter the structure of the oligomeric species. The kinetics of fibril formation is monitored through a Thioflavin T fluorescence assay. Global fitting of the kinetic data indicates that secondary nucleation plays a key role in the aggregation of the Ac-PHF6-NH2 tau segment, while the primary nucleation rate is greatly accelerated by heparin.
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