Friday, February 3, 2023
SCIENMAG: Latest Science and Health News
No Result
View All Result
  • Login
  • HOME PAGE
  • BIOLOGY
  • CHEMISTRY AND PHYSICS
  • MEDICINE
    • Cancer
    • Infectious Emerging Diseases
  • SPACE
  • TECHNOLOGY
  • CONTACT US
  • HOME PAGE
  • BIOLOGY
  • CHEMISTRY AND PHYSICS
  • MEDICINE
    • Cancer
    • Infectious Emerging Diseases
  • SPACE
  • TECHNOLOGY
  • CONTACT US
No Result
View All Result
Scienmag - Latest science news from science magazine
No Result
View All Result
Home SCIENCE NEWS Chemistry AND Physics

Structure of Parkinson’s protein could lead to new diagnostic and treatment options

March 28, 2016
in Chemistry AND Physics
0
Share on FacebookShare on Twitter
IMAGE

CHAMPAIGN, Ill. — Chemists have identified the complex chemical structure of the protein that stacks together to form fibrils in the brains of Parkinson's disease patients. Armed with this knowledge, researchers can identify specific targets for diagnosis and treatment.

University of Illinois chemists, collaborating with peers at the University of Pennsylvania, Vanderbilt University and Queen Mary University of London, detailed their mapped structure of the protein in the journal Nature Structural and Molecular Biology.

In Parkinson's, the protein alpha-synuclein forms long fibrils that disrupt brain activity. This is similar to the beta-amyloid fibrils that form in Alzheimer's disease patients. However, while the beta-amyloid structure is known, the alpha-synuclein structure has eluded researchers as a result of its complexity, its insolubility and the difficulty of characterizing one protein within a fibril.

"This is the first structure of the full-length fibril protein, which is now well established to be important for the pathology of Parkinson's disease," said study leader Chad Rienstra, a University of Illinois chemistry professor. "Knowing that structure will open up many new areas of investigation for diagnosing and treating Parkinson's disease."

The Illinois group used a special type of molecular imaging called magic-angle spinning nuclear magnetic resonance to measure the placement of atoms in six different samples of alpha-synuclein. In each set of samples, they looked at different sets of atoms, then used advanced computational power to put them all together like pieces of a giant jigsaw puzzle.

"We had to find patterns in the data and systematically test all the possibilities for how the protein would fit together," Rienstra said. "It's like when you solve a really complex puzzle, you know you have it right at the end because all the pieces fit together. That's what we got with this structure."

See a video on YouTube at https://www.youtube.com/watch?v=tZjXeAfqGG4.

The group experimentally verified the structure with collaborators by producing the protein in the lab and checking it with various imaging methods to see if it matched the fibrils found in Parkinson's patients. They also verified it biologically by testing it in cell cultures and seeing that it indeed behaved like the protein found in patients.

"These structures are crucial for understanding the mechanisms for how Parkinson's disease works," said Marcus Tuttle, first author of the paper, who worked on the project as a graduate researcher in Rienstra's group and is now a postdoctoral fellow at Yale University. "Amyloid diseases are incredibly complex systems. What structural features drive pathology? That's a super interesting question, but until now there's been no structure. Now there's a whole avenue where we can start to explore the basic mechanism of how the protein works."

Rienstra's group is working with the Michael J. Fox Foundation to identify possible diagnostic agents that could target certain spots on the alpha-synuclein protein and would "light up" in a brain scan, allowing for earlier and more accurate diagnosis.

"We think that the structure that we resolved of alpha-synuclein fibrils will be really significant in the immediate future and has use for diagnosing Parkinson's in patients before they're symptomatic," Rienstra said. "Once people start having symptoms, whether of Alzheimer's or Parkinson's, in many ways it's a little too late to be effective with therapy. But if you catch it early, I think there's a lot of promise for therapies that are being developed. Those are all relying upon the structures that we're solving."

###

The National Institutes of Health supported this work.

Editor's notes: To reach Chad Rienstra, call (217) 244-4655; email [email protected]

The paper "Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein" is available online or from the News Bureau.

Media Contact

Liz Ahlberg
[email protected]
217-244-1073
@NewsAtIllinois

http://www.illinois.edu

Share25Tweet16Share4ShareSendShare
  • cotton microfiber

    Looking beyond microplastics, Oregon State researchers find that cotton and synthetic microfibers impact behavior and growth of aquatic organisms

    70 shares
    Share 28 Tweet 18
  • Seawater split to produce green hydrogen

    70 shares
    Share 28 Tweet 18
  • Feather mite species related to the Laysan albatross discovered in Japan

    65 shares
    Share 26 Tweet 16
  • Voice-activated system for hands-free, safer DNA handling

    65 shares
    Share 26 Tweet 16
  • Why lung cancer doesn’t respond well to immunotherapy

    65 shares
    Share 26 Tweet 16
  • Face masks cut distance airborne pathogens could travel in half, new study finds

    183 shares
    Share 73 Tweet 46
ADVERTISEMENT

About us

We bring you the latest science news from best research centers and universities around the world. Check our website.

Latest NEWS

New study shows snacking on mixed tree nuts may impact cardiovascular risk factors and increase serotonin

Null results research now published by major behavioral medicine journal

Looking beyond microplastics, Oregon State researchers find that cotton and synthetic microfibers impact behavior and growth of aquatic organisms

Subscribe to Blog via Email

Enter your email address to subscribe to this blog and receive notifications of new posts by email.

Join 205 other subscribers

© 2022 Scienmag- Science Magazine: Latest Science News.

No Result
View All Result
  • HOME PAGE
  • BIOLOGY
  • CHEMISTRY AND PHYSICS
  • MEDICINE
    • Cancer
    • Infectious Emerging Diseases
  • SPACE
  • TECHNOLOGY
  • CONTACT US

© 2022 Scienmag- Science Magazine: Latest Science News.

Welcome Back!

Login to your account below

Forgotten Password?

Retrieve your password

Please enter your username or email address to reset your password.

Log In