Suyun biçimlendirdiği sıcak nokta tau proteinlerinin kümelenmesini başlatıyor

Tau proteins can misfold and assemble into long fibrils that disrupt communication between neurons, a process associated with Alzheimer’s disease and related tauopathies. A Northwestern-led study reports that vulnerable tau has one dominant hotspot that begins this recruitment process. At the hotspot, water forms a dynamic cap around a water-repelling, or hydrophobic, part of the protein. When a soluble tau molecule approaches the matching spot on another tau or at a fibril end, release of this water helps pull the two sites together. The incoming molecule then adopts the misfolded shape and extends the fibril. The researchers tested the idea by placing a chemical tag over the hotspot: fibril growth stopped, unlike when they tagged two other sites away from it. The work does not provide a dementia treatment, but it identifies a specific interaction that could guide future diagnostic models and therapies. It may also help scientists make laboratory fibrils that more closely imitate disease-associated forms of tau.