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Rational Structure‐Based Design of Fluorescent Probes for Amyloid Folds

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Author Orts Julien, Wälti Marielle Aulikki, Ghosh Dhiman, Campioni Silvia, Saupe Sven J., Riek Roland,
Project Molecular and Cellular Modulation in Parkinson's Disease
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Original article (peer-reviewed)

Journal chembiochem
Volume (Issue) 20
Page(s) 0 - 0
Title of proceedings chembiochem
DOI 10.1002/cbic.201800664

Open Access

URL https://onlinelibrary.wiley.com/doi/full/10.1002/cbic.201800664
Type of Open Access Green OA Embargo (Freely available via Repository after an embargo)

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.
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