The Scope E-Newsletter April 2009

Valerie Berthelier, PhD, Director, Conformational Diseases and Therapeutics Research, Assistant Professor, Medicine, and Adjunct Professor, UT/ORNL Graduate Program for Genome Science and Technology, and her team believe that the culprit is hidden in the middle of a malfunctioning process.

Healthy proteins in our body fold in order to perform their many tasks, such as supporting the skeleton, controlling senses, moving muscles and others, but sometimes, proteins fold improperly and therefore malfunction. Misfolded proteins are responsible for many diseases, including Huntington’s. Researchers believed for years that aggregates of a specific misfolded protein neutralized neuronal cell functions, causing the neurodegenerative disease and killing the cells. Dr. Berthelier and her team, however, agree with contemporary research that the true and devastating damage occurs in the steps before the aggregation takes place. Locating the precise location and stimulating a change in the process are the active work of the team.

"We work to identify compounds that can stabilize intermediate stages of the aggregation process in order to study them and determine if they are toxic," Dr. Berthelier said. "Compounds can be used to change the structure of the aggregate, rather than prevent its formation, allowing healthy cells to destroy it. The work is rewarding and holds promise for therapeutics in the future."

This work has been praised by the National Institutes of Health, which awarded Dr. Berthelier’s work in 2007 a sizeable grant. The lab’s breakthrough work also has caught the attention of Oak Ridge National Laboratories, which now work in partnership with Dr. Berthelier and provide significant funding as well.