Characteristics of the binding of thioflavin S to tau paired helical filaments.
Binding of histological benzothiazole dye thioflavin S (ThS) to protein aggregates has been related with the presence of amyloid beta 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.
Santa-María
Ismael
I
Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Universidad Autónoma de Madrid, Cantoblanco, 28049-Madrid, Spain.
Pérez
Mar
M
Hernández
Félix
F
Avila
Jesús
J
Moreno
Francisco J
FJ
D000544:Alzheimer Disease / Q000378:metabolism; D019138:Antibodies, Blocking / Q000494:pharmacology; D052160:Benzothiazoles; D005455:Fluorescent Antibody Technique; D019763:Heparin Lyase / Q000494:pharmacology; D006801:Humans; D008854:Microscopy, Electron; D008856:Microscopy, Fluorescence; D016900:Neurofilament Proteins / Q000378:metabolism*; D011485:Protein Binding; D011809:Quinones / Q000494:pharmacology; D013844:Thiazoles / Q000378:metabolism*; D016875:tau Proteins / Q000378:metabolism*
D019138:Antibodies, Blocking; D052160:Benzothiazoles; D016900:Neurofilament Proteins; D011809:Quinones; D013844:Thiazoles; D016875:tau Proteins; C009462:thioflavin T; D019763:Heparin Lyase