Health News | Study Finds Copper Causes Protein Aggregation, May Cause Parkinson's Disease | NewestLY

Washington [US], July 9 (ANI): Exposure to copper in the environment and the protein alpha-synuclein in the human brain may play an important role in the pathogenesis of Parkinson’s disease. The researchers were able to show how the protein takes on an unusual shape when exposed to large amounts of copper ions. These findings could help develop new strategies for the treatment of neurodegenerative diseases.

The causes of Parkinson’s disease are not fully understood. Long before the onset of characteristic muscle tremors, the appearance of faulty proteins in the brain can be the first sign. Researchers at Empa and the University of Limerick in Ireland have now taken a closer look at the abnormal shape of these alpha-synucleins in the form of a protein ring. By doing so, they were also able to visualize at the nanoscale the relationship with environmental pollution by copper. It highlights the development of neurodegenerative diseases and the role of biometals in the disease process. In addition, the findings may provide opportunities to improve early detection and therapy of the disease.

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Suspicious metal

What is known about Parkinson’s disease is that neurons in the brain die, resulting in a deficiency of the neurotransmitter dopamine. In the later stages of the disease, this causes muscle tremors, muscle rigidity, and even immobility. Slow progressive disease is the second most common neurodegenerative disease in the world after Alzheimer’s disease. Environmental factors such as pesticides or metals can trigger Parkinson’s.

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The team led by Empa researcher Peter Nirmalraj from the Transport laboratory at Nanoscale Interfaces is investigating this hypothesis using imaging and chemical spectroscopy techniques and, in collaboration with Damien Thompson’s team at the University of Limerick, computer simulations. The researchers targeted a protein involved in several molecular processes in the development of Parkinson’s: alpha-synuclein. In affected individuals, these endogenous proteins clump together and cause nerve cells to die. The researchers suspect that high concentrations of copper interfere with this process and accelerate the disease process.

crime ring

To visualize the clumping of alpha-synuclein at the nanometer scale, researcher Empa Silvia Campioni of the Cellulose & Wood Materials laboratory produced the protein artificially. Using an atomic force microscope, the researchers were then able to observe the protein, initially in solution, for ten days as it formed an insoluble filamentous structure before eventually clumping together to form a dense network of fibrils. Based on the images, the transformation of soluble protein into agglomerated fibers about 1 micrometer long, as occurs during disease progression, can be observed with impressive precision in the laboratory.

If the researchers then added copper ions to the protein solution, a completely different structure appeared under the microscope: Ring-shaped protein structures about 7 nanometers in size, called oligomers, appeared in test tubes in just a few hours. The existence of ring-shaped oligomers and their cell-damaging effects are well known. What’s more, the longer fiber-like structure appeared earlier than the copper-free solution.

“On the one hand, high doses of copper seem to speed up the aggregation process,” said Peter Nirmalraj. Moreover, however, this unusual ring-shaped protein structure develops relatively quickly under the influence of copper, which may mark the beginning of the pathological process or even trigger it. The researchers also analyzed the binding of copper ions to alpha-synuclein using molecular dynamics computer simulations in tiny steps of 10 to 100 nanoseconds.

Pre-test

Since oligomeric rings are formed early in protein transformation, they can be used as targets for new forms of therapy, Nirmalraj hopes. In addition, these findings could help advance the development of a Parkinson’s test that can detect disease at an early stage in body fluids, for example by using samples from spinal fluid. (ANI)

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