2005 Zenith Fellows Award

Alzheimer’s disease is characterized by abnormal structures composed of beta-amyloid protein fragments. Studies have shown that beta-amyloid molecules assemble themselves in particular stages, eventually forming the well-characterized amyloid plaques. In recent years, scientists identified oligomers, an early stage of this assembly process, composed of just a few beta-amyloid molecules. Evidence suggests that oligomers may be the primary toxic agent in Alzheimer’s disease.

Single beta-amyloid molecules and oligomers have properties that make it difficult for researchers to study them in isolation, not the least of which is their propensity to assemble themselves into larger structures. H. Eugene Stanley, Ph.D., and colleagues are approaching this problem by integrating more traditional biochemical laboratory experiments and computer modeling.

Their goal is to investigate properties of beta-amyloid molecules and oligomers and to create atomic-level models that demonstrate how the molecules are designed for assembly and how they actually assemble themselves. Their investigation may reveal structural elements that are critical for beta-amyloid assembly and that may be viable targets for new disease-modifying therapies.