Professor David S. Eisenberg
Post Doctoral Fellows
I am working on determining structures of Tau oligomers and amyloid fibers that are involved in Alzheimer’s disease and other tauopathies. Through these studies I hope to uncover the structural basis of toxicity and seeding, as well as to understand how certain Tau structures might protect against disease. Additionally I am working with Lin Jiang to develop inhibitors that block Tau fibrillization based on structures that our group has solved.
As a postdoctoral researcher at UCLA, I am in charge of planning and executing a fundamental science research program to understand biochemical processes of systemic amyloidosis disease, and build a foundation for development of a possible cure of the disease in future. Amyloidosis develops due to assembly of light-chain immunoglobulins into a protein polymer, known as amyloid fibrils. These fibrils possess a special biochemical properties preventing their clearance from the body, eventually leading to essential organs failure and death.
Recent research had shown that propagation of amyloid fibrils is mediated by a discrete, naturally occurring short peptide segments with a high propensity to assemble into insoluble beta-sheet structures. With a goal of illuminating the structural basis of systemic amyloidosis, I hypothesized that such peptide segments exist in immunoglobulin light-chains. In concordance with this hypothesis, I identified several peptide segments within lambda type immunoglobulins that induce formation of amyloid-like structures. Currently, I use a site-directed mutagenesis methods to assess the structural necessity of these peptide segments to light-chain immunoglobulin amyloidogenic potential, in hope to use this data for development of molecules that will disrupt amyloid formation, which is the ultimate long term goal of our research.
I am a postdoc in Eisenberg’s lab and my research here mostly focuses on the interaction between Amyloid beta (Aβ) and its binders (binding proteins/small molecules). My goal is to solve the crystal structure of binder stabilized Aβ (or Aβ derived peptides), or developing Aβ inhibitors from these binding protein/small molecules.
My research focuses on determining the molecular structures of Amyloid Beta (Aβ), the protein responsible for Alzheimer’s Disease. Aβ is observed as multiple aggregated structures including amyloid fibrils, smaller protofibrils, as well as oligomeric species which are associated with higher toxicities. By determining the structures of the distinct species, I hope to identify what features are responsible for Aβ toxicity. To this end, I have focused on familial mutations in Aβ which alter the structure and contribute to heightened toxicity and early onset of the disease.
I help people to determine and analyze interesting macromolecular structures by crystallography. I assist with data collection, data processing, phasing, model building and structure interpretation, and teach others about these techniques.
Boston University Class of 2014, BA in Chemistry, minor in Mathematics