ArticleThe journal of physical chemistry letters2022
Controlling Amyloid Fibril Properties Via Ionic Liquids: The Representative Case of Ethylammonium Nitrate and Tetramethylguanidinium Acetate on the Amyloidogenesis of Lysozyme.
Article in The journal of physical chemistry letters, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 17 citations in OpenAlex.
- Kelvin Probe Force Microscopy in Bionanotechnology: Current Advances and Future Perspectives.Advanced materials (Deerfield Beach, Fla.) · 2026Review
- Ionic Liquid-Enabled Drug Delivery Systems: Benefits, Limitations, and Future Perspectives.Pharmaceutics · 2026Review
- Solvation of Model Biomolecules in Choline-Aminoate Ionic Liquids: A Computational Simulation Using Polarizable Force Fields.Molecules (Basel, Switzerland) · 2024Article
- Ionic liquids meet lipid bilayers: a state-of-the-art review.Biophysical reviews · 2023Review
- Delamination of Layered Double Hydroxide in Ionic Liquids under Ambient Conditions.The journal of physical chemistry letters · 2022Article
- Influence of Metal Salts Addition on Physical and Electrochemical Properties of Ethyl and Propylammonium Nitrate.International journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein aggregation into amyloid fibrils has been observed in several pathological conditions and exploited in nanotechnology. It is also key in several biochemical processes. In this work, we show that ionic liquids (ILs), a vast class of organic electrolytes, can finely tune amyloid properties, opening a new landscape in basic science and applications. The representative case of ethylammonium nitrate (EAN) and tetramethyl-guanidinium acetate (TMGA) ILs on lysozyme is considered. First, atomic force microscopy has shown that the addition of EAN and TMGA leads to thicker and thinner amyloid fibrils of greater and lower electric potential, respectively, with diameters finely tunable by IL concentration. Optical tweezers and neutron scattering have shed light on their mechanism of action. TMGA interacts with the protein hydration layer only, making the relaxation dynamics of these water molecules faster. EAN interacts directly with the protein instead, making it mechanically unstable and slowing down its relaxation dynamics.
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Registered trials
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