David S. Eisenberg

(310) 825-3754

201A Boyer Hall
611 Charles E. Young Drive East
Los Angeles, CA 90095
Phone: 310-825-3754

Position Titles

Distinguished Professor, Biological Chemistry
Chair, Paul D. Boyer Professor of Biochemistry and Molecular Biology
Investigator, Howard Hughes Medical Institute


David Eisenberg is currently Professor of Chemistry and Biochemistry and Biological Chemistry, as well as HHMI Investigator.  Before he came to UCLA, Eisenberg earned an A.B. in Biochemical Sciences from Harvard College and a D.Phil. from Oxford University in Theoretical Chemistry on a Rhodes Scholarship. After postdoctoral study at Princeton University on water and hydrogen bonding and at Caltech on protein crystallography, he joined the faculty at UCLA. Currently he studies protein interactions by X-ray crystallography, bioinformatics, and biochemistry, with an emphasis on amyloid-forming proteins. This recently recognized protein state offers opportunities to understand cells in health and disease, and in synthesizing new materials and in understanding processes as diverse as biofilms and corrosion. Eisenberg has published over 300 papers and reviews, holds half a dozen patents.

Research Description

David Eisenberg and his research group focus on protein interactions. In their experiments they study the structural basis for conversion of normal proteins to the amyloid state and conversion of prions to the infectious state. In bioinformatic work, they derive information on protein interactions from genomic and proteomic data, and design inhibitors of amyloid toxicity.

Amyloid and prion diseases are diseases of protein aggregation in which a normal, functional protein converts to an abnormal, aggregated protein. The systemic amyloid diseases, such as dialysis-related amyloidosis, are apparently caused by the accumulation of fibers until organs fail. The neurodegenerative amyloid diseases, such as Alzheimer’s, Parkinson’s, amyotrophic lateral sclerosis (ALS), and the prion conditions, seem to be caused by smaller oligomers, intermediate in size between monomers and fibers. Our goals are to understand the general features of the conversion to the amyloid state, why some of the diseases are transmissible between organisms and others not, what the structures of the toxic units are, and how they exert their toxic actions, and how to interfere with amyloid toxicity.

Awards & Honors

2015- ADBMB Bert and Natalie Vallee Award in Biomedical Science
2013- International Society for Computational Biology ISCB Award
2010- Honorary Fellow, Queen’s College, Oxford
2009- Technion – Israel Institute of Technology Harvey Prize in Human Health
2009- Biophysical Society Emily Gray Award
2009- Amer Chemical Society Preceptor for the Nobel Laureate Signature Award
2008- Biophysical Society Emily M. Gray Award (with Donald Crothers)
2005- Harvard Westheimer Medal
2004- UCLA Seaborg Medal
2001- Howard Hughes Medical Institute Investigator
2000- The Protein Society Amgen Award
1998- Amer Chemical Society Repligen Award in Molecular Biology
1997- African-American Male Achiever Network Honoree
1997- Biophysical Society National Lecture Award
1996- Protein Society Stein & Moore Award
1992- The Immunotoxin Society Pierce Award
1989- National Academy of Sciences Elected Member
1982- UCLA McCoy Award
1975- UCLA Distinguished Teaching Award
1972- U.S. Public Health Service USPHS Career Development Award
1961-1964 Oxford University Rhodes Scholarship
1961- Harvard University L.J. Henderson Prize
1960 Harvard Scholarship Honorary Scholarships: Phi Beta Kappa; Sigma Xi