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Alpha-synuclein is a nuclear and synaptic protein that is expressed abundantly in the brain (it is 1% of the total brain’s protein). This protein is involved in regulating neurotransmission, synaptic function, and neuroplasticity. However, when this protein is deformed and folded, it tends to accumulate and form intracellular aggregates called Lewy bodies (CL) and Lewy neurites (NL).
These aggregates play a fundamental role in the development of Parkinson's disease, a neurodegenerative disorder that affects more than 10 million people worldwide. This disorder is characterized by the appearance of motor symptoms such as tremors, rigidity, and bradykinesia caused by the loss of dopaminergic neurons from the substance nigra pars compacta. So far, there is no known treatment for the disease, but there is new research that could find a new way.
A New Approach to α-synuclein
According to a study published in the journal Nature, researchers at Brigham and Women's Hospital in Boston have discovered the structural key to α-synuclein, which could prevent the progression and even development of degeneration in neurons caused by Parkinson's disease. In the study, it is claimed that the protein may have a radically different structure in healthy cells than had been observed so far.
Dennis Selkoe, one of the leaders of the research, states: “The data show that α-synuclein is erroneously characterized as a native form of protein that lacks structure (...) This discovery is of fundamental importance in understanding both how α-synuclein normally works and how this protein is altered in Parkinson's”.
Proteins are chains of amino acids folded into three-dimensional chains. The function of the protein determines the shape of the string. The study suggests that this is precisely what happens with α-synuclein in its innocuous form, and in its pathological conformation that forms the Lewy bodies present in patients with the disease.
Scientists have always assumed that α-synuclein is produced as a monomer. However, Selkoe's team has shown that protein has a more sophisticated form. In the 1990s, the protein was stable when exposed to conditions that usually alter the structure of most proteins. The researchers designed experiments to analyze the behavior of α-synuclein, using milder methods, to better understand the grouping behavior of the protein.
The results showed that the protein is tetrameric and that this is the predominant form in healthy human cells. In this form, the protein presents a remarkable resistance to aggregation. The tetramers maintained their original structure for ten days throughout the experiment.
According to Selkoe: “Our hypothesis is that the folded protein must be disassembled into monomers before being able to form large pathological aggregates (...) if the soluble tetrameric synuclein can be maintained, it may be able to prevent the progress and even the development of Parkinson's neuronal degeneration”.
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