A study published in the journal Nature Partner Journal - Parkinson's disease, has unearthed a series of protein structures believed to be closely associated with the onset of Parkinson's disease. Researchers from the University Bath in the UK hoped that further analysis of the unique structures may open up new avenues in the treatment of the disease.
Dr. Beckie Port, research manager at Parkinson's UK, said, "By advancing our understanding of the different structures of the protein that are likely to be present inside brain cells, this University of Bath study helps pave the way for developing treatments that may one day stop the progression of Parkinson's."
According to Parkinson's UK, more than 1 million people in the UK are affected by the disease - either by living with the condition, or as a friend, colleague, or family member of someone who is. The latest estimates show that in 2020, around 145,000 people live with a Parkinson's diagnosis in the UK.
The disease is characterized by a specific protein 'misfolding', where it becomes distorted and then malfunctions. The protein which researchers at Bath have studied - alpha-synuclein (Î±S) - is abundant in all human brains. After misfolding, it accumulates in large masses, known as Lewy bodies. These masses consist of slender Î±S fibers that are toxic to dopamine-producing brain cells, causing them to die. It is this drop in dopamine that triggers the symptoms of Parkinson's Disease.
There has been much research into Î±S structure and the role it plays in Parkinson's, however, virtually all studies have taken place in laboratory test tubes, where the protein is purified from bacteria and studied in isolation. Research of this kind often overlooks the fact that in the living brain, Î±S fibers form in the presence of 'phospholipids' - large fatty substances that make up cell membranes and play an essential role in living cells, both in their structure and metabolism.
New Era In Parkinson's Research
Professor Jody Mason and his team from the Department of Biology & Biochemistry examined how Î±S misfolds in the presence of phospholipids. They discovered a series of misfolded protein structures that have never been observed before. These Î±S fibers were larger than any previously reported and took on a striking variety of shapes. Some formed flat ribbons, others appeared as long, wave-like helices, while others still were more compact and bulkier.
The Bath researchers hope their discovery will mark the start of a new era in Parkinson's research. Their work lays the foundation for a detailed analysis of misfolded Î±S fibers. Once the structure of these fibers is better understood, scientists will be able to investigate which versions are disease-causing and which are not.
Increased Interest In Structures
From here, they will be able to test drugs against pathogenic forms. This will constitute a major step forward in finding a cure for Parkinson's and other neurological conditions. "We know that these misfolded proteins are heavily implicated in Parkinson's disease," said Professor Mason.
The research charity Parkinson's UK has invested over Â£3.5 million in understanding the role played in the brain by Î±S. It recognizes that unlocking the secrets of this protein could hold the key to finding a cure for the condition.
Port, said, "Alpha-synuclein is known to form different structures, and researchers have become increasingly interested in which forms of the protein may be toxic and linked to the spread and loss of brain cells in Parkinson's - this is essential in order to develop treatments that target the right form of the protein.
(With inputs from agencies)