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Rational Structure‐Based Design of Fluorescent Probes for Amyloid Folds
Author(s) -
Orts Julien,
Aulikki Wälti Marielle,
Ghosh Dhiman,
Campioni Silvia,
Saupe Sven J.,
Riek Roland
Publication year - 2019
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800664
Subject(s) - amyloid (mycology) , amyotrophic lateral sclerosis , rational design , amyloid fibril , chemistry , biophysics , neuroscience , biochemistry , medicine , biology , disease , amyloid β , nanotechnology , pathology , materials science
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.