Creating a free account will enable you to subscribe to our daily and weekly email newsletters, as well as customize your reading experience to show only the categories most relevant to you.
Signing up only take a few minutes, so why not give it a try and see what you've been missing out on.
Researchers have taken detailed images and measurements of the morphing structure of a brain protein thought to play a role in Parkinson's disease, information that could aid the development of medications to treat the condition.
The protein, called alpha synuclein (pronounced sine-yoo-cline), ordinarily exists in a globular shape. However, the protein morphs into harmful structures known as amyloid fibrils, which are linked to protein molecules that form in the brains of patients with neurodegenerative diseases.
"The abnormal protein formation characterizes a considerable number of human diseases, such as Alzheimer's, Parkinson's and Huntington's diseases and type II diabetes," said Lia Stanciu, an associate professor of materials engineering at Purdue University.
Until now, the transition from globular to fibrils had not been captured and measured.
Researchers incubated the protein in a laboratory and then used an electron microscope and a technique called cryoelectron microscopy to snap thousands of pictures over 24 hours, capturing its changing shape. The protein was frozen at specific time intervals with liquid nitrogen.
Findings reveal that the protein morphs from its globular shape into "protofibril" strands that assemble into pore-like rings. These rings then open up, forming pairs of protofibrils that assemble into fibrils through hydrogen bonds.
"We found a correlation between protoﬁbrils in these rings and the ﬁbrils, for the ﬁrst time to our knowledge, by measuring their true sizes and visualizing the aggregation steps," Stanciu said. "A better understanding of the mechanism yields fresh insight into the pathogenesis of amyloid-related diseases and may provide us the opportunity to develop additional therapeutic strategies."
Parkinson's disease affects 1 percent to 2 percent of people older than 60, and an increase in its prevalence is anticipated in coming decades.
The findings were detailed in a research paper appearing in the June issue of the Biophysical Journal. The paper was authored by doctoral student Hangyu Zhang; former postdoctoral research associate Amy Griggs; Jean-Christophe Rochet, an associate professor of medicinal chemistry and molecular pharmacology; and Stanciu.
The researchers caused the protein to morph into fibrils by exposing it to copper, mimicking what happens when people are exposed to lead and other heavy metals. The contaminants interfere with the protein, changing the oxidation states of ions in its structure.
The research was funded by the National Institutes of Health. Future work will include experiments focusing on what happens when higher concentrations of copper are used.
Written by Emil Venere
Article adapted by Medical News Today from original press release. Click 'references' tab above for source.
Visit our Parkinson's Disease category page for the latest news on this subject.
Please use one of the following formats to cite this article in your essay, paper or report:
Emil Venere, Purdue University. "Research yields first detailed view of morphing Parkinson's protein." Medical News Today. MediLexicon, Intl., 9 Sep. 2013. Web.
19 Apr. 2014. <http://www.medicalnewstoday.com/releases/265798>
Emil Venere, Purdue University. (2013, September 9). "Research yields first detailed view of morphing Parkinson's protein." Medical News Today. Retrieved from
Please note: If no author information is provided, the source is cited instead.
If you write about specific medications, operations, or procedures please do not name healthcare professionals by name.
For any corrections of factual information, or to contact our editorial team, please use our feedback form. Please send any medical news or health news press releases to:
Note: Any medical information published on this website is not intended as a substitute for informed medical advice and you should not take any action before consulting with a health care professional. For more information, please read our terms and conditions.
This page was printed from: http://www.medicalnewstoday.com/releases/265798.php
Visit www.medicalnewstoday.com for medical news and health news headlines posted throughout the day, every day.
© 2004-2014 All rights reserved. MNT is the registered trade mark of MediLexicon International Limited.