Journal
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
Volume 13, Issue 30, Pages 7058-7064Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpclett.2c01505
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This study reveals that ionic liquids can finely adjust the properties of amyloid fibrils, expanding the realm of basic science and applications. By investigating the effects of ethylammonium nitrate and tetramethyl-guanidinium acetate ionic liquids on lysozyme, it is found that they can modify the thickness, electric potential, and diameter of amyloid fibrils, and the mechanism of their action is elucidated.
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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