By examining the interaction of types of polarized light with the alpha-synuclein protein, they observed rearrangements of the protein on the molecular level prior to aggregation. In addition, the researchers identified early events in the assembly of these structures. The new Cornell experiments paint stunning visual evidence of a wide array of protein aggregates with varying molecular structures, some of which might be key to understanding Parkinson's disease. (See accompanying electron nanoscopic images.) The research shows that the aggregates maybe involved in infiltrating healthy cells and causing disease, which could result in toxicity. "These ringlike annular aggregates have been seen with atomic force microscopy before, and people have been interested in them for a long time," said Valerie Anderson, first author and a graduate student in Webb's lab. These structures, some long and thin, and others inter-wound or spooled, could suggest alternative pathways to alpha-synuclein aggregation in the brain. Using chemical solutions of fluorinated alcohol to trigger protein structural transitions, the researchers observed the formation of irregular, helical aggregates that may be similar to formations in the brain of Parkinson's disease patients. Webb and Weill Cornell biochemistry professor David Eliezer, aimed to shed light on structural changes in alpha-synuclein. The Cornell group, led by applied and engineering physics professor Watt W. Many researchers surmise that smaller clusters (known as oligomers or aggregates) of alpha-synuclein protein could be responsible for initiating neurodegeneration. But it is still unclear whether Lewy bodies are a symptom of the disease or are themselves responsible for cell death. Parkinson's disease patients have dense lesions in their midbrains called Lewy bodies, which involve aggregates of alpha-synuclein. 2 edition of Proceedings of the National Academy of Sciences (online Oct. By retracing the history of each abnormal reaction, biochemists aim to determine the events that lead to disease and to intervene in the process.Ĭollaborative research between Ithaca-based Cornell applied physicists and biochemists at Weill Cornell Medical College has yielded new clues into what happens when the Parkinson's disease-associated protein alpha-synuclein undergoes abnormal aggregation. But, they also can misbehave in myriad ways. Proteins perform almost every function our bodies require for life.
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