Refined Peptide Seeks Out Root Cause Of Parkinson's Disease

Misfolding alpha-synuclein (αS) proteins are considered key players in the development of Parkinson's disease, giving rise to toxic clumps called Lewy bodies that kill off important brain cells, Nick Lavars reported for New Atlas.

Photo Insert: Scientists at the University of Bath researching Parkinson's treatment have now achieved a breakthrough with the development of a finely engineered peptide that produced "very exciting" results in early experiments.

As such, research focuses on preventing this type of protein dysfunction, and scientists at the University of Bath have now achieved a breakthrough with the development of a finely engineered peptide that produced "very exciting" results in early experiments. The research was published in the Journal of Molecular Biology.

Lewy bodies are associated with a range of neurological diseases, but their role in the onset of Parkinson's is tied to their tendency to kill neurons that produce the neurotransmitter dopamine.

The death of these cells and decline in dopamine is what drives the deterioration of motor control seen in Parkinson's sufferers, such as tremors and slowness of movement.

The development of drugs that intervene in this process by targeting αS is a highly active area of research and one where scientists are making some promising strides. Recent advances in the space include molecules that help the brain seek and destroy the misfolding proteins, molecular tweezers that can pull the clumps apart, and artificial enzymes that prevent them from spreading.

The University of Bath team has been pursuing a peptide-based solution to this problem, screening more than 200,000 of the chains of amino acids in search of one that can prevent αS misfolding.

This led them to a peptide called 4554W, which stopped αS from developing into toxic clumps in laboratory experiments on live cells.

“Previous attempts to inhibit αS aggregation with small molecule drugs have been unfruitful as they are too small to inhibit such large protein interactions," says Dr Richard Meade, the study lead author. "This is why peptides are a good option – they are big enough to prevent the protein from aggregating but small enough to be used as a drug."

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