Ricardo Maccioni, Ph.D.
International Center for Biomedicine
Santiago, Chile

2008 Investigator-Initiated Research Grant

The protein tau normally plays a vital role in maintaining the structural framework and transportation system within nerve cells. Tau is modified by a process called phosphorylation, or the adding of phosphate molecules. During Alzheimer's disease, however, tau becomes excessively phosphorylated and tends to accumulate into harmful structures called neurofibrillary tangles. These tangle formations prevent tau from carrying out its normal functions and may damage nerve cells.

Scientists do not yet understand exactly how neurofibrillary tangles are formed. Abnormal tau likely interacts with various molecules that play a role in tangle development. Research teams are looking to identify these molecules and to understand how they interact with tau.

In preliminary research, Ricardo Maccioni, Ph.D., and colleagues found that molecules called benzimidazoles attach themselves to aggregated forms of tau protein. Furthermore, these molecules have properties that may enable them to effectively "highlight" tau tangles on brain scans. For their proposed study, Dr Maccioni and colleagues will use cultured cells to analyze how certain benzimidazoles interact with tau. They will also test the molecule's ability to visually highlight tau.

Results of Dr. Maccioni's effort could lead to a better understanding of neurofibrillary tangle formation. The work could also identify a novel imaging technique for diagnosing Alzheimer's disease.