ScienceDaily (July 23, 2012) ? A team of University of Alberta researchers has identified a new class of compounds that inhibit the spread of prions, misfolded proteins in the brain that trigger lethal neurodegenerative diseases in humans and animals.
U of A chemistry researcher Frederick West and his team have developed compounds that clear prions from infected cells derived from the brain.
"When these designer molecules were put into infected cells in our lab experiments, the numbers of misfolded proteins diminished -- and in some cases we couldn't detect any remaining misfolded prions," said West.
West and his collaborators at the U of A's Centre for Prions and Protein Folding Diseases say this research is not yet a cure, but does open a doorway for developing treatments.
"We're not ready to inject these compounds in prion-infected cattle," said David Westaway, director of the prion centre. "These initial compounds weren't created for that end-run scenario but they have passed initial tests in a most promising manner."
West notes that the most promising experimental compounds at this stage are simply too big to be used therapeutically in humans or animals.
Human exposure to prion-triggered brain disorder is limited to rare cases of Creutzfeldt-Jakob or mad cow disease. The researchers say the human form of mad cow disease shows up in one in a million people in industrialized nations, but investigating the disease is nonetheless well worth the time and expense.
"There is a strong likelihood that prion diseases operate in a similar way to neurodegenerative diseases such as Alzheimer's, which are distressingly common around the world," said West.
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The above story is reprinted from materials provided by University of Alberta, via EurekAlert!, a service of AAAS.
Note: Materials may be edited for content and length. For further information, please contact the source cited above.
Journal Reference:
- Charles E. Mays, Shaon Joy, Lei Li, Linghui Yu, Sacha Genovesi, Frederick G. West, David Westaway. Prion inhibition with multivalent PrPSc binding compounds. Biomaterials, 2012; 33 (28): 6808 DOI: 10.1016/j.biomaterials.2012.06.004
Note: If no author is given, the source is cited instead.
Disclaimer: This article is not intended to provide medical advice, diagnosis or treatment. Views expressed here do not necessarily reflect those of ScienceDaily or its staff.
Source: http://www.sciencedaily.com/releases/2012/07/120723134856.htm
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