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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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Ionic Radii03:10

Ionic Radii

33.8K
Ionic radius is the measure used to describe the size of an ion. A cation always has fewer electrons and the same number of protons as the parent atom; it is smaller than the atom from which it is derived. For example, the covalent radius of an aluminum atom (1s22s22p63s23p1) is 118 pm, whereas the ionic radius of an Al3+ (1s22s22p6) is 68 pm. As electrons are removed from the outer valence shell, the remaining core electrons occupying smaller shells experience a greater effective nuclear...
33.8K
Ionic Bonds00:42

Ionic Bonds

131.7K
Overview
When atoms gain or lose electrons to achieve a more stable electron configuration they form ions. Ionic bonds are electrostatic attractions between ions with opposite charges. Ionic compounds are rigid and brittle when solid and may dissociate into their constituent ions in water. Covalent compounds, by contrast, remain intact unless a chemical reaction breaks them.
Opposing Charges Hold Ions Together in Ionic Compounds
Ionic bonds are reversible electrostatic interactions between ions...
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Molecular and Ionic Solids02:54

Molecular and Ionic Solids

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Crystalline solids are divided into four types: molecular, ionic, metallic, and covalent network based on the type of constituent units and their interparticle interactions.
Molecular Solids
Molecular crystalline solids, such as ice, sucrose (table sugar), and iodine, are solids that are composed of neutral molecules as their constituent units. These molecules are held together by weak intermolecular forces such as London dispersion forces, dipole-dipole interactions, or hydrogen bonds, which...
20.2K
Solubility of Ionic Compounds02:55

Solubility of Ionic Compounds

68.3K
Solubility is the measure of the maximum amount of solute that can be dissolved in a given quantity of solvent at a given temperature and pressure. Solubility is usually measured in molarity (M) or moles per liter (mol/L). A compound is termed soluble if it dissolves in water.
68.3K
Ionic Crystal Structures02:42

Ionic Crystal Structures

17.7K
Ionic crystals consist of two or more different kinds of ions that usually have different sizes. The packing of these ions into a crystal structure is more complex than the packing of metal atoms that are the same size.
Most monatomic ions behave as charged spheres, and their attraction for ions of opposite charge is the same in every direction. Consequently, stable structures for ionic compounds result (1) when ions of one charge are surrounded by as many ions as possible of the opposite...
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Updated: Feb 11, 2026

Pretreatment of Lignocellulosic Biomass with Low-cost Ionic Liquids
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Suppression and dissolution of amyloid aggregates using ionic liquids.

Takahiro Takekiyo1, Yukihiro Yoshimura2

  • 1Department of Applied Chemistry, National Defense Academy, 1-10-20, Hashirimizu, Yokosuka, Kanagawa, 239-8686, Japan. take214@nda.ac.jp.

Biophysical Reviews
|April 27, 2018
PubMed
Summary

Ionic liquids show promise for treating neurodegenerative diseases by suppressing amyloid formation and dissolving harmful protein aggregates. Their interaction with amyloid proteins and hydrogen-bonding ability are key to this effect.

Keywords:
Amyloid aggregatesDissolutionIonic liquidsProtein–IL interactionSolution structureSuppression

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Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis
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Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis
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Area of Science:

  • Biochemistry
  • Neuroscience
  • Materials Science

Background:

  • Amyloid aggregates, characterized by β-sheet structures, are implicated in neurodegenerative diseases.
  • Developing treatments requires suppressing and dissolving these insoluble protein aggregates.
  • Ionic liquids (ILs) are known to inhibit protein aggregation and dissolve water-insoluble substances.

Purpose of the Study:

  • To review the effects of ionic liquids (ILs) on suppressing and dissolving amyloid aggregates.
  • To explore the potential of ILs as therapeutic agents for neurodegenerative diseases.
  • To understand the mechanisms behind ILs' interaction with amyloid proteins.

Main Methods:

  • Literature review of studies investigating ionic liquids and amyloid aggregates.
  • Analysis of the biochemical basis for ILs' effects on amyloid formation and dissolution.
  • Examination of protein-IL affinity and ILs' hydrogen-bonding basicity.

Main Results:

  • Ionic liquids demonstrate both suppression of amyloid formation and dissolution of amyloid aggregates.
  • Protein-IL affinity is identified as the mechanism for suppressing amyloid formation.
  • Hydrogen-bonding basicity of ILs is proposed as the mechanism for dissolving amyloid aggregates.

Conclusions:

  • Ionic liquids show significant potential as novel pharmaceuticals for neurodegenerative diseases.
  • ILs can serve as effective recovery agents for various amyloid aggregates.
  • Further research into ILs could lead to new therapeutic strategies for amyloid-related disorders.