• Aβ42 fibrils and oligomers (inset) visualized by electron microscopy
  • Neurons (NeuN) and astrocytes (GFAP) in a tauopathy mouse brain
  • Dendritic spines depleted by Aβ42 and rescued by CLR01
  • Amyloid plaques and neurofibrillary tangles in a mouse brain before and after treatment with CLR01
  • Aβ40 fibrils and oligomers (inset) visualized by electron microscopy
  • Insulin microcrystals in the absence (A) or presence (B) of CLR01
  • Islet amyloid polypeptide fibrils and oligomers (inset) visualized by electron microscopy
  • Time-dependent change in the circular dichroism spectrum of Aβ during aggregation

Gal Bitan, Ph.D.
Professor of Neurology
David Geffen School of Medicine at UCLA



Our main research focus is the abnormal self-association of proteins into toxic oligomers, aggregates, and amyloid fibrils and the involvement of these aberrant protein assemblies in human diseases. We study the molecular interactions involved in these processes and explore novel tools to inhibit the formation of the toxic assemblies.

Abnormal protein oligomerization and aggregation cause, or are involved in, over 30 diseases called amyloidoses or proteinopathies. Of this large family of diseases, we study mainly Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis (ALS). Another focus of our lab is analysis of biomarkers that can improve the diagnosis and facilitate drug development for these diseases.

One of our major projects is the development of "Molecular Tweezers" as novel drug candidates for proteinopathies. We are leading a project called Breakthrough Treatment for Degenerative Diseases (www.BTDD.org) that involves collaboration with multiple laboratories at UCLA and around the world.