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Neurodegenerative diseases distinguished through protein-structure analysis

Parkinson’s disease and multiple system atrophy involve the protein α-synuclein. Proof that aggregated α-synuclein adopts a different structure in each case suggests that its conformation underlies the distinct disorders.
  1. Juan Atilio Gerez

    1. Juan Atilio Gerez is in the Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, ETH-Hönggerberg, 8093 Zurich, Switzerland.

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  2. Roland Riek

    1. Roland Riek is in the Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, ETH-Hönggerberg, 8093 Zurich, Switzerland.

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A snowflake begins life as a tiny crystal that acts as a seed on which water molecules aggregate, increasing the size of the snowflake as it descends to earth. Proteins can also act as seeds — for instance, in a class of age-related disorders called amyloid diseases, in which thousands of copies of a type of protein known as an amyloid adopt an abnormal structure and aggregate in harmful clumps. In Parkinson’s disease, aggregates of the amyloid protein α-synuclein accumulate in neurons. A rarer neurodegenerative disease, multiple system atrophy (MSA), involves α-synuclein aggregates in neuron-supporting cells called glia. It can be difficult to distinguish between the two disorders, given their overlapping symptoms, but they require different treatments. Writing in Nature, Shahnawaz et al.1 provide an explanation for this difference: like two dissimilar snowflakes composed of identical water molecules, α-synuclein aggregates form distinct 3D architectures in each disease.

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Nature 578, 223-224 (2020)

doi: https://doi.org/10.1038/d41586-020-00131-3

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