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Suppression and dissolution of amyloid aggregates using ionic liquids

Suppression and dissolution of amyloid aggregates using ionic liquids Amyloid aggregates are composed of protein fibrils with a dominant β-sheet structure, are water-insoluble, and are involved in the pathogenesis of many neurodegenerative diseases. Development of pharmaceuticals to treat these diseases and the design of recovery agents for amyloid-type inclusion bodies require the successful suppression and dissolution of such aggregates. Since ionic liquids (ILs) are composed of both a cation and anion and are known to suppress protein aggregation and to dissolve water-insoluble compounds such as cellulose; they may also have potential use as suppression/dissolution agents for amyloid aggregates. In the following review, we present the suppression and dissolution effects of ILs on amyloid aggregates so far reported. The protein–IL affinity (the ability of ILs to interact with amyloid proteins) was found to be the biochemical basis for ILs’ suppression of amyloid formation, and the hydrogen-bonding basicity of ILs might be the basis for their ability to dissolve amyloid aggregates. These findings present the potential of ILs to serve as novel pharmaceuticals to treat neurodegenerative diseases and as recovery agents for various amyloid aggregates. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biophysical Reviews Springer Journals

Suppression and dissolution of amyloid aggregates using ionic liquids

Biophysical Reviews , Volume 10 (3) – Apr 25, 2018

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References (62)

Publisher
Springer Journals
Copyright
Copyright © 2018 by International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature
Subject
Life Sciences; Biochemistry, general; Biological and Medical Physics, Biophysics; Cell Biology; Membrane Biology; Biological Techniques; Nanotechnology
ISSN
1867-2450
eISSN
1867-2469
DOI
10.1007/s12551-018-0421-8
Publisher site
See Article on Publisher Site

Abstract

Amyloid aggregates are composed of protein fibrils with a dominant β-sheet structure, are water-insoluble, and are involved in the pathogenesis of many neurodegenerative diseases. Development of pharmaceuticals to treat these diseases and the design of recovery agents for amyloid-type inclusion bodies require the successful suppression and dissolution of such aggregates. Since ionic liquids (ILs) are composed of both a cation and anion and are known to suppress protein aggregation and to dissolve water-insoluble compounds such as cellulose; they may also have potential use as suppression/dissolution agents for amyloid aggregates. In the following review, we present the suppression and dissolution effects of ILs on amyloid aggregates so far reported. The protein–IL affinity (the ability of ILs to interact with amyloid proteins) was found to be the biochemical basis for ILs’ suppression of amyloid formation, and the hydrogen-bonding basicity of ILs might be the basis for their ability to dissolve amyloid aggregates. These findings present the potential of ILs to serve as novel pharmaceuticals to treat neurodegenerative diseases and as recovery agents for various amyloid aggregates.

Journal

Biophysical ReviewsSpringer Journals

Published: Apr 25, 2018

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