Glycan Determinants of Heparin-Tau Interaction.

ABSTRACT: Tau aggregates into paired helical filaments within neurons, a pathological hallmark of Alzheimer's disease. Heparin promotes tau aggregation and recently has been shown to be involved in the cellular uptake of tau aggregates. Although the tau-heparin interaction has been extensively studied, little is known about the glycan determinants of this interaction. Here, we used surface plasmon resonance (SPR) and NMR spectroscopy to characterize the interaction between two tau fragments, K18 and K19, and several polysaccharides, including heparin, heparin oligosaccharides, chemically modified heparin, and related glycans. Using a heparin-immobilized chip, SPR revealed that tau K18 and K19 bind heparin with a K_D of 0.2 and 70 μM, respectively. In SPR competition experiments, N-desulfat

SUBMITTER: Zhao J 

PROVIDER: S-EPMC5355497 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature