The theory, if verified by other researchers, could help focus efforts to develop preventive drugs, according to the study's lead researcher, Chi Ming Yang, Ph.D., a professor of chemistry at Nankai University in Tianjin, China. In Alzheimer's disease, another neurodegenerative disease, the amyloid precursor protein has been implicated. Normally, the body can clear itself of free radicals. But with age, this system may fail. When enough free radicals accumulate to damage a protein molecule, it can malfunction, he says.
Proteins typically fold into specific three-dimensional structures that determine their functions.
A malfunctioning protein may remain partially unfolded, which can place different amino acids in close proximity, Yang explained. In the case of Alzheimer's and prion diseases, the reductive amino acids in close proximity can lead to the formation of protein plaques, according to Yang. Although Alzheimer's and prion diseases seem to start in similar ways, they progress differently. This may explain why Alzheimer's disease advances at a much slower pace than Creutzfeldt-Jakob disease, says Yang. A nonprofit organization with a membership of 161,000 chemists and chemical engineers, the American Chemical Society publishes scientific journals and databases, convenes major research conferences, and provides educational, science policy and career programs in chemistry.