Effects of Charged Polyelectrolytes on Amyloid Fibril Formation of a Tau Fragment.

ABSTRACT: The microtubule-associated protein tau is involved in more than 20 different neurological disorders characterized by aberrant intracellular aggregation of tau in the brain. Here, we investigated the aggregation of a novel 20-residue model peptide, tau_298-317, which is derived from the key microtubule binding domain of the full sequence tau. Our results show that tau_298-317 highly mimics the physical and aggregation properties of tau. Under normal physiological conditions, the peptide maintains a disordered random coil without aggregation. The presence of polyanionic heparin (Hep) significantly promotes the aggregation of this peptide to form amyloid fibrils. The Hep-induced aggregation is sensitive to the ionic strength of the solution and the introduction of the nega

SUBMITTER: Islam M 

PROVIDER: S-EPMC10249396 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature