A highly selective and specific PET tracer for imaging of tau pathologies

J Alzheimers Dis. 2012;31(3):601-12. doi: 10.3233/JAD-2012-120712.


Senile plaques and neurofibrillary tangles are prominent neuropathological hallmarks in Alzheimer's disease and are considered to be targets for therapeutic intervention as well as biomarkers for diagnostic in vivo imaging agents. While there are a number of amyloid-β positron emission tomography (PET) tracers currently in different stages of clinical development and commercialization, there have been very few reports on imaging agents selectively targeting tau aggregates. In search of [18F]-PET tracers that possess great binding affinity and selectivity toward tau tangles, we tested more than 900 compounds utilizing a unique screening process. A competitive autoradiography assay was set up to test compounds for binding to native tau tangles and amyloid-β plaques on human brain tissue sections. In our in vitro assays, the 18F labeled compound [18F]-T808 displayed a high level of binding affinity and good selectivity for tau aggregates over amyloid-β plaques. [18F]-T808 showed rapid uptake and washout in rodent brains. Our in vitro and preclinical in vivo studies suggest that [18F]-T808 possesses suitable properties and characteristics to be a specific and selective PET probe for imaging of paired helical filament tau in human brains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Peptides / metabolism
  • Animals
  • Autoradiography / methods
  • Fluorine Radioisotopes* / metabolism
  • Humans
  • Mice
  • Mice, Inbred ICR
  • Plaque, Amyloid / diagnostic imaging
  • Plaque, Amyloid / metabolism
  • Positron-Emission Tomography / methods*
  • Protein Binding / physiology
  • Radiopharmaceuticals* / chemistry
  • Radiopharmaceuticals* / metabolism
  • Rats
  • Rats, Sprague-Dawley
  • tau Proteins* / metabolism


  • Amyloid beta-Peptides
  • Fluorine Radioisotopes
  • MAPT protein, human
  • Radiopharmaceuticals
  • tau Proteins