The Potential of Small Molecules in Preventing Tau Oligomer Formation and Toxicity

J. E. Gerson, Filippa Lo Cascio, Rakez Kayed

Research output: Chapter in Book/Report/Conference proceedingChapter

4 Scopus citations


The accumulation of pathological protein deposits, amyloids, in neurodegenerative disease represents a formidable challenge for drug development. With no effective treatment in sight, and recent findings suggesting that protein aggregates are diverse, dynamic, and capable of spreading, it is crucial that researchers find safe and successful therapeutic approaches that target the most toxic amyloid species. The pathological aggregation of microtubule-associated protein tau has been identified as a critical factor in the progression of Alzheimer's disease and other neurodegenerative disorders. More evidence continues to come to light to suggest that soluble, intermediate tau aggregates-tau oligomers-are the most toxic species in disease and may be responsible for the spread of pathology, rather than neurofibrillary tangles, the primary tauopathy hallmark, suggesting that oligomeric tau may be the best therapeutic target. Here we discuss the potential of small molecules in preventing amyloid and tau oligomer toxicity and future directions.

Original languageEnglish (US)
Title of host publicationNeuroprotection in Alzheimer's Disease
PublisherElsevier Inc.
Number of pages25
ISBN (Electronic)9780128037126
ISBN (Print)9780128036907
StatePublished - Jan 20 2017


  • Amyloid
  • Pathological tau
  • Small molecules
  • Tau aggregation
  • Tau oligomers

ASJC Scopus subject areas

  • Medicine(all)
  • Neuroscience(all)


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