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

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

 

 

Research

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 50 diseases called amyloidoses or proteinopathies. Of this large family of diseases, we study  Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis (ALS), and others. Another focus of our lab is the analysis of biomarkers that can improve the diagnosis and facilitate drug development for these diseases. In this context, we are interested in biomarkers in extracellular vesicles (EVs) originating in the CNS and isolated from peripheral bio fluids. We also study how EVs mediate transfer of biological material among cells and the consequences of such delivery.

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.