In contrast, Tau fibrils had limitedeffects on αSyn aggregation in synucleinopathy mouse models(M20). Previous studies have shown thatthe non-amyloid-β component (NAC) core of αSyn (residues61–95) can serve as an inducer of Tau polymerization, emphasizingthe crucial role of β-sheets in their cross-seeding., The current study found that mixed and hybrid αSyn/Tau PFFsgenerated more secondary structures and displayed higher seeding potencythan pure αS. This evidence concerns the gene PPIB and synucleinopathy.