Effect of Tau Fragment and Membrane Interactions on Membrane Permeabilization and Peptide Aggregation.

ABSTRACT: Aggregation of tau protein is a hallmark feature of tauopathies such as Alzheimer's disease. The microtubule-binding domain of tau plays a crucial role in the tau aggregation process. In this study, we investigated the dual effects of membrane interactions of tau_298-317, a fragment peptide from the microtubule-binding domain, on peptide-induced membrane disruption and membrane-mediated peptide self-assembly. Our results show that neither wild-type tau_298-317 nor its P301L or Ser305-phosphorylated mutants aggregate in the presence of zwitterionic POPC vesicles or cause lipid vesicle leakage, indicating weak peptide-membrane interactions. In contrast, tau_298-317 strongly interacts with negatively charged POPG liposomes, leading to a rapid transition of the pe

SUBMITTER: Islam M 

PROVIDER: S-EPMC12297872 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature