Phosphorylation modulates the local conformation and self‐aggregation ability of a peptide from the fourth tau microtubule‐binding repeat

摘要: Phosphorylation of tau protein modulates both its physiological role and aggregation into paired helical fragments, as observed in Alzheimer's diseased neurons. It is fundamental importance to study fragment formation modulation by phosphorylation. This focused on the fourth microtubule-binding repeat tau, encompassing an abnormal phosphorylation site, Ser356. The propensities this peptide corresponding phosphorylated form were investigated using turbidity, thioflavin T fluorescence electron microscopy. There evidence for a conformational change upon phosphorylation, well changes activity. Although peptides have ability aggregate, weaker peptide. reveals that are capable self-aggregation at Ser356 can modulate process.