Cryo-EM structure of alpha-synuclein fibrils.

Journal: eLife

Published: 2018-07-03

DOI: 10.7554/elife.36402

Affiliations: 4

Authors: 8

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Research Highlight

Determining the structure of Parkinson’s disease

© KATERYNA KON/SCIENCE PHOTO LIBRARY/Getty

© KATERYNA KON/SCIENCE PHOTO LIBRARY/Getty

Protein fibrils thought to be one the culprits behind Parkinson’s disease have been imaged in detail for the first time.

Parkinson’s disease is a degenerative disorder that mainly affects the part of the brain responsible for movement. The protein alpha-synuclein, when it accumulates in needle-like fibrils in the brain, is believed to be one of factors that trigger the disease. But until recently, no-one had succeeded in determining the atomic structure of an entire fibril.

Now, a team that included researchers at Roche Pharma Research and Early Development made an alpha-synuclein fibril in a test tube and then used cyro-electron microscopy to image its structure at an atomic resolution. They found that the proteins in the fibril form a helical structure.

This structural knowledge could help researchers to develop a way to diagnose the crippling disease earlier.

Supported content

  1. eLife 7, e36402 (2018). doi: 10.7554/eLife.36402
Institutions FC
Center for Cellular Imaging and NanoAnalytics (C-CINA), UB, Switzerland 0.50
Roche Pharma Research and Early Development (Roche pRED), Switzerland 0.38
Laboratory of Physical Chemistry (LPC), ETH Zurich, Switzerland 0.13

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