Rational Structure-Based Design of Fluorescent Probes for Amyloid Folds
- Author(s)
- Julien Orts, Marielle Aulikki Wälti, Dhiman Ghosh, Silvia Campioni, Sven J Saupe, Roland Riek
- Abstract
Amyloid fibrils are pathological hallmarks of various human diseases, including Parkinson's, Alzheimer's, amyotrophic lateral sclerosis (ALS or motor neurone disease), and prion diseases. Treatment of the amyloid diseases are hindered, among other factors, by timely detection and therefore, early detection of the amyloid fibrils would be beneficial for treatment against these disorders. Here, a small molecular fluorescent probe is reported that selectively recognize the fibrillar form of amyloid beta(1–42), α-synuclein, and HET-s(218–289) protein over their monomeric conformation. The rational design of the reporters relies on the well-known cross-β-sheet repetition motif, the key structural feature of amyloids.
- Organisation(s)
- External organisation(s)
- Eidgenössische Technische Hochschule Zürich, Eidgenössische Materialprüfungs- und Forschungsanstalt, Université Bordeaux
- Journal
- ChemBioChem: a european journal of chemical biology
- Volume
- 20
- Pages
- 1161-1166
- No. of pages
- 6
- ISSN
- 1439-4227
- DOI
- https://doi.org/10.1002/cbic.201800664
- Publication date
- 05-2019
- Peer reviewed
- Yes
- Austrian Fields of Science 2012
- 106006 Biophysics, 106002 Biochemistry
- Keywords
- ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all), Molecular Medicine, Molecular Biology, Biochemistry, Organic Chemistry
- Sustainable Development Goals
- SDG 3 - Good Health and Well-being
- Portal url
- https://ucris.univie.ac.at/portal/en/publications/rational-structurebased-design-of-fluorescent-probes-for-amyloid-folds(76a389c4-af53-4258-be0b-213b120551fe).html