For those without a medical or biological science background, the mechanisms of disease can be mysterious. The nature of disease and its beginnings as a microscopic irregularity can seem like a strange and complex phenomenon. There are many diseases that researchers are still searching for answers about.

Parkinson's disease is a prime example of a disease that has remained markedly mysterious, even after years of meticulous research. Without a thorough understanding of what occurs within the human brain to trigger the onset of the disease, it can be very difficult to treat. However, a new study may provide some clarification into this particularly complex disorder. 

How Protein Aggregation Contributes

Parkinson's disease is a progressive, neurodegenerative syndrome. Deterioration of neurons causes the onset of neurological symptoms. With Parkinson's, these symptoms can include tremors, slowed movement, impaired posture and balance, and changes in speech and writing. Scientists have isolated aggregation of the protein alpha-synuclein as a significant factor linked to the onset of some of these symptoms. 

Before protein aggregation progresses and forms amyloid filaments, proteins experience an intermediary stage. At this point, proteins are present as oligomers - non-repeating, non-aggregating molecules. The mechanisms that trigger the oligomers to aggregate, form amyloid filaments, and begin neurological degradation is a hot topic of study and debate. 

New Research Around Protein Aggregation

A person with Parkinson's experiences general progression of the disease throughout the duration of their life. However, the process of movement from one protein stage to another happens extremely slowly. A new study, performed by researchers at the University of Virginia School of Medicine in conjunction with the Federal University of Rio de Janeiro, Brazil, attempts to understand the mechanisms that cause Parkinson's patients to progress from one protein stage to the next. 

In the study, researchers use fluorescent light to provide progressive bioimaging of four variants of the alpha-synuclein protein - three from early-onset cases of the disease and one from individuals with advanced age. They found significant differences in the development of oligomeric proteins and the overall rate of protein aggregation. Overall, they found that oligomers developed at a much more aggressive rate in early-onset cases of the disease.

After uncovering the results of the initial bioimaging, researchers applied cryo-electron microscopy to view the molecular structure of amyloid filaments. They found that a certain protein mutation species participated much more frequently in amyloid filament growth, marking them as proteins significant to filament growth. Moreover, researchers noted the amyloid filaments had distinctive structures that seemed to result from the particular protein mutation from which they originated.

Conclusions About Protein Aggregation

From this research, scientists believe that, with more observation of how proteins change over time, isolation of the exact mechanisms that promote the onset of changes can be identified. The study was able to identify the beginning stages of protein aggregation and the formation of amyloid filaments in early-onset cases with a family history of the disease. It is hoped that a better understanding of these aggregations and the associations that form them can provide insight into how to prevent them from forming in the first place. 

With more time and research stemming from the results of this study, the prevention of amyloid filaments may be able to stop neurodegeneration in its tracks.