Protein Biochemistry and Neuroenzymology - Terrone L. Rosenberry

Overview

Dr. Rosenberry and his laboratory colleagues study three components from human brain that may play roles in Alzheimer's disease (AD). One component, β-amyloid (Aβ), is composed of 40- and 42-residue Aβ peptides. The brains of AD patients contain large numbers of Aβ amyloid fibrils in the form of senile plaques. It now appears likely that Aβ peptides and fibrillar Aβ aggregates play an important role in the development of AD, and therapeutic strategies that prevent aggregate formation are attractive. Since cellular interfaces affect aggregation rates and aggregate structures, we are investigating the ways in which several interfaces, including polar-nonpolar interfaces and anionic micellar surfaces, alter aggregation in vitro. Interfaces in general promote aggregation by bringing Aβ peptides into closer proximity, but some interfaces also selectively stabilize Aβ42 aggregates called oligomers. We propose that inhibitors of Aβ aggregation or promoters of Aβ disaggregation in vitro will reduce the amyloid burden in AD patients. To test this proposal, we are investigating selected monoclonal antibodies and peptides that prevent or reverse the assembly or growth of Aβ aggregates.

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