David S. Eisenberg is a Professor of Chemistry and Biochemistry and Biological Chemistry at the University of California, Los Angeles, where he also serves as Director of the UCLA-DOE Institute for Genomics and Proteomics and as an HHMI Investigator. His research focuses on protein interactions, particularly the structural basis for conversion of normal proteins to the amyloid state and conversion of prions to the infectious state. Dr. Eisenberg earned his undergraduate degree in biochemical sciences from Harvard College and his D.Phil. degree in theoretical chemistry from Oxford University on a Rhodes Scholarship. His postdoctoral research was on ice and water with Walter Kauzmann at Princeton and in protein crystallography with Richard Dickerson. He joined the UCLA faculty after his postdoctoral studies. Dr. Eisenberg and his research group focus on protein interactions in amyloid and prion diseases. These diseases involve protein aggregation where normal functional proteins convert to abnormal aggregated forms. Systemic amyloid diseases like dialysis-related amyloidosis result from fiber accumulation until organ failure, while neurodegenerative diseases like Alzheimer's, Parkinson's, ALS, and prion conditions appear to be caused by smaller oligomers. In 2005, his team determined the atomic-level structure for the amyloid fiber spine, revealing a 'steric zipper' of two parallel beta sheets packed across a dry interface. Since then, they've determined approximately 90 amyloid spines from 15 disease-related proteins. In 2010, they identified the structure of a toxic amyloid-related oligomer consisting of six anti-parallel beta strands forming a cylindrical barrel. His recent publications demonstrate continued innovation in amyloid research, with focus areas including structural prediction of amyloid formation, mechanisms of tau fibril disassembly in Alzheimer's disease, cryo-EM analysis of amyloid polymorphism, and structure-based design of inhibitors for amyloid toxicity. His work integrates computational, structural, and biochemical approaches to understand protein aggregation across multiple disease contexts. Dr. Eisenberg has received numerous prestigious awards and honors: National Academy of Sciences Member American Philosophical Society Member Institute of Medicine Member Howard Hughes Medical Institute Investigator Biophysical Society Emily M. Gray Award Harvard Westheimer Medal UCLA Seaborg Medal Technion - Israel Institute of Technology Harvey Prize in Human Health As Director of the UCLA-DOE Institute for Genomics and Proteomics and an HHMI Investigator, Dr. Eisenberg leads significant research initiatives in protein structure and aggregation. His laboratory combines X-ray crystallography, bioinformatics, and biochemical techniques to investigate protein interactions, with particular emphasis on amyloid-forming proteins and their role in disease. The Eisenberg Lab, located in Boyer Hall at UCLA, maintains an active research program investigating the structural basis of protein aggregation. The lab continues to build on its landmark discoveries of amyloid structures while exploring new frontiers in understanding protein misfolding diseases and developing potential therapeutic interventions.
