David Eisenberg, PhD, studies the structure and action of proteins in the amyloid state with the goal of diagnosing and treating amyloid diseases, such as Parkinson's disease (PD). His laboratory was the first to determine high-resolution structures of the sticky segments of amyloid-forming proteins. One of such segments is NACore, the core of the NAC domain of alpha-synuclein, a sticky protein that clumps in the brains of people with Parkinson's disease (PD). From the atomic-resolution structures of these segments, Dr. Eisenberg and his colleagues designed inhibitors of amyloid fibril formation, i.e., chemicals that slow the process. So far, the researchers have been developing inhibitors of fibrils of several proteins, including tau, a protein associated with Alzheimer's disease and some 25 other diseases called tauopathies; alpha-synuclein, which is associated with Parkinson's disease; IAPP, associated with type 2 diabetes; and transthyretin, associated with transthyretin amyloidosis.
One of the present goals of the laboratory, in collaboration with Massoud Akhtari, PhD, of UCLA, is to attach the inhibitor of alpha-synuclein to magnetic nanoparticles to create a novel diagnostic tool capable of safely monitoring the growth and inhibition of alpha-synuclein fibrils.