Shortened α-synuclein fibrils are formed in the interaction with copper ions
Korean researchers have demonstrated a copper-based supramolecular approach for unraveling the formation process of pathogenic α-synuclein (αSyn) fibrils in the brain and its application in a neurotoxic mechanism study, opening the door to new treatment options that could stop or slow Parkinson`s disease and other neurodegenerative disorders.
New research led by Professor Hugh Kim at Korea University and Professor Lee Min-jae at Seoul National University found that copper ions retard the elongation of αSyn fibrils unlike typical αSyn fibrillation, leading to the formation of shortened αSyn fibrils that are rapidly transmitted and accumulated to neuronal cells, causing neurotoxicity and neuronal cell death. This non-canonical self-assembly of αSyn provides the supramolecular basis for generating pathogenic amyloid assemblies.
Copper has been shown previously to bind to αSyn to induce αSyn aggregation and the structural variation of αSyn fibrils has been linked to the diverse etiologies of synucleinopathies. However, little had been known about what specific mechanism αSyn fibrils provides with pathologic features, researchers said.
Parkinson`s disease is a neurodegenerative disorder that slowly destroys neurons in the brain that are essential for controlling movement. This is caused by neurotoxicity from the aggregation of αSyn proteins in the brain.
The study was published in Angewandte Chemie International Edition on Feb. 16.
By Kim Yoon-jin and Minu Kim
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