"Tiny Tau" manuscript published in Nature Chemistry
The aggregation of tau is a hallmark of many neurological disorders. Recent studies have shown that misfolded tau propagates its conformation in a similar way as prions. In this paper, we found that a 31-residue fragment of tau (R3 domain) rapidly forms amyloid fibrils in vitro and exhibits "prion-like" behavior by seeding full length tau aggregation in a cellular model system. We also demonstrated that subtle changes in R3 significantly affect the "prion" activity. Further studies by fiber diffraction, HDX, FTIR, and SSNMR provided detailed structural information of this transmissible form.
Highlighted in Alzforum (http://www.alzforum.org/news/research-news/does-taus-third-repeat-propag...)