The laboratory's two major research projects are focused on understanding these key components in the nervous system: (1) the role of β-amyloid (Aβ) in Alzheimer's disease (AD) and (2) the structure and catalytic properties of the enzyme acetylcholinesterase (AChE).

Since β-amyloid protein molecules tend to self-associate, the first project focuses on the structure of aggregates. Small soluble aggregates called oligomers are of particular interest because they are thought to initiate pathological changes that lead to AD. Several biophysical techniques are applied in these studies, but foremost are solid-state NMR and cryoelectron microscopy. These studies involve intensive interactions with faculty collaborators at Georgia Tech and Florida State University. An immediate goal is the determination of the structure of oligomers formed on small anionic micelles.

The second project investigates the interaction of several inhibitors with the AChE catalytic site and interprets them in the context of the known 3D structure of AChE. A variety of kinetic studies have been designed to distinguish inhibitor interactions with an enzyme peripheral site from those at the active site catalytic triad. An important goal is to identify peripheral site inhibitors that can modulate AChE reactions at the catalytic triad.


About Dr. Rosenberry

Terrone L. Rosenberry, Ph.D., is an emeritus professor of pharmacology at Mayo Clinic College of Medicine and Science in Jacksonville, Florida. Still actively engaged in research, Dr. Rosenberry and his colleagues study pathological components that are present in the brains of patients with Alzheimer's disease to determine how to inhibit or block their occurrence. They also investigate the catalytic mechanism of the brain enzyme acetylcholinesterase.