Alzheimer’s disease is the most common human neurodegenerative disorder, affecting as many as 5.1 million people in America alone. Alzheimer’s leads to progressive and irreversible memory loss, disability and, eventually, death through a complex series of events that take place in the brain over a period of many years.
In the nucleus of nearly every human cell, long strands of DNA are packed tightly together to form chromosomes. To deliver these instructions to various other cellular structures, the chromosomes dispatch very small protein fibers – called oligomers – that fold into three-dimensional shapes. Misfolded proteins – called amyloid fibrils – cannot function properly and tend to accumulate into tangles and clumps of waxy plaque, robbing brain cells of their ability to operate and communicate with each other.
“The exact mechanism of amyloid formation and the origin of its toxicity are not fully understood, primarily due to a lack of sufficient atomic-level structuralinformation from traditional experimental approaches,” explained Jie Zheng, Ph.D., an assistant professor of chemical and biomolecular engineering at the University of Akron. “Molecular simulations, in contrast, allow one to study the three-dimensional structure and its kinetic pathway of amyloid oligomers at full atomic resolution.”
Zheng’s research group is leveraging the computational muscle of the IBM Cluster 1350 system at the Ohio Supercomputer Center to develop a multiscale modeling and simulation platform that aims to establish a direct correlation between the formation of oligomers and their biological activity in cell membranes.
Project lead: Jie Zheng, University of Akron
Research title: Exploring kinetics and structures of Alzheimer’s amyloid .-protein formation
Funding source: National Science Foundation