Abstract
<p indent="0mm">Alzheimer’s disease (AD) is a common cause of dementia among elders. Hyperphosphorylation and aggregation of Tau correlate with the clinical progression of AD. In this study, the Thioflavin T fluorescence spectroscopy was used to explore the aggregation kinetics of pTau protein <italic>in vitro</italic>. The effects of pTau oligomer seeds, temperature, metal ions, and macromolecular crowding agents on the aggregation kinetics were also studied. The results indicated that the aggregation of pTau protein accords with the sigmoidal equation of the nucleation-elongation model. The presence of oligomer seeds, increase in temperature, addition of Al<sup>3+</sup>, and macromolecular crowding reagents considerably promote the aggregation of pTau protein. Moreover, the effect on the rate of pTau nucleation was stronger than that of elongation.
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