Affiliations: Centro de Biología Molecular “Severo Ochoa” (CSIC-UAM), Universidad Autónoma de Madrid, Cantoblanco, 28049-Madrid, Spain
Correspondence:
[*]
Corresponding authors: Francisco J. Moreno or Jesús Avila, Centro de Biología Molecular “Severo Ochoa”, Facultad de Ciencias. Campus de Cantoblanco, Universidad Autónoma de Madrid, 28049-Madrid, Spain. Tel.: +34 914978460; Fax: +34 914974799; E-mail: [email protected], [email protected].
Abstract: Binding of histological benzothiazole dye thioflavin S (ThS) to protein aggregates has been related with the presence of amyloid β sheet structure in those protein aggregates. Paired helical filaments (PHF) from Alzheimer's disease (AD) patients, (whose main component is the microtubule associated protein, tau) bind to thioflavins. By using a novel immunofluorescence method, the binding of ThS to isolated tau filaments was tested. Also, the characteristics of this binding of ThS to PHF or to the in vitro assembled tau filaments, have been analyzed. Our results suggests that ThS binds to PHF with a higher affinity than to the straight filaments (SF), also found in AD.
