Controlling Amyloid Fibril Properties Via Ionic Liquids: The Representative Case of Ethylammonium Nitrate and Tetramethylguanidinium Acetate on the Amyloidogenesis of Lysozyme

Visakh V S Pillai, Pallavi Kumari, Srikanth Kolagatla, Victoria Garcia Sakai, Svemir Rudić, Brian J Rodriguez, Marina Rubini, Katarzyna M Tych, Antonio Benedetto*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

5 Downloads (Pure)

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.

Original languageEnglish
Pages (from-to)7058-7064
Number of pages7
JournalThe Journal of Physical Chemistry Letters
Volume13
Early online date28-Jul-2022
DOIs
Publication statusPublished - 28-Jul-2022

Cite this