TY - JOUR
T1 - Controlling Amyloid Fibril Properties Via Ionic Liquids
T2 - The Representative Case of Ethylammonium Nitrate and Tetramethylguanidinium Acetate on the Amyloidogenesis of Lysozyme
AU - Pillai, Visakh V S
AU - Kumari, Pallavi
AU - Kolagatla, Srikanth
AU - Garcia Sakai, Victoria
AU - Rudić, Svemir
AU - Rodriguez, Brian J
AU - Rubini, Marina
AU - Tych, Katarzyna M
AU - Benedetto, Antonio
PY - 2022/7/28
Y1 - 2022/7/28
N2 - 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.
AB - 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.
U2 - 10.1021/acs.jpclett.2c01505
DO - 10.1021/acs.jpclett.2c01505
M3 - Article
C2 - 35900133
SN - 1948-7185
VL - 13
SP - 7058
EP - 7064
JO - The Journal of Physical Chemistry Letters
JF - The Journal of Physical Chemistry Letters
ER -