Avoiding Misfolding

  • Author: David Bradley
  • Published: 26 February 2011
  • Copyright: Wiley-VCH Verlag GmbH & Co. KGaA
  • Source / Publisher: Journal of Medicinal Chemistry/ACS Publications
thumbnail image: Avoiding Misfolding

US researchers have identified 2-aminothiazoles as possible non-toxic lead compounds in the search for a pharmaceutical to treat prion diseases, such as Creutzfeldt-Jakob Disease (CJD). Prions are infectious agent composed of protein in a misfolded form. They duplicate themselves as proteins misfold in the brain leading to lethal deposits and holes in brain tissue.

Tests on the 2-aminothiazoles-based compounds in mice suggest that they can cross the blood-brain barrier and in laboratory tests show activity against abnormal protein accumulation. Protein misfolding is also present in Alzheimer’s disease, Huntington’s disease, Parkinson’s disease. Prion diseases are invariably fatal, and no viable treatments are currently available.

Article Views: 2961

Sign in Area

Please sign in below

Additional Sign In options

Please note that to comment on an article you must be registered and logged in.
Registration is for free, you may already be registered to receive, e.g., the newsletter. When you register on this website, please ensure you view our terms and conditions. All comments are subject to moderation.

Article Comments - To add a comment please sign in

If you would like to reuse any content, in print or online, from ChemistryViews.org, please contact us first for permission and consult our permission guidance prior to making your request

Follow on Facebook Follow on Twitter Follow on YouTube Follow on LinkedIn Follow on Instagram RSS Sign up for newsletters

Magazine of Chemistry Europe (16 European Chemical Societies) published by Wiley-VCH