Effect of 1-Ethyl-3-methylimidazolium Tetrafluoroborate and Acetate Ionic Liquids on Stability and Amyloid Aggregation of Lysozyme

• Published in: International journal of molecular sciences 2022-01, Vol.23 (2), p.783
• Main Authors: Fedunova, Diana, Antosova, Andrea, Marek, Jozef, Vanik, Vladimir, Demjen, Erna, Bednarikova, Zuzana, Gazova, Zuzana
• Format: Article
• Language: English
• Subjects: Acetates - chemistry; Acetic acid; Amyloid; Amyloid - chemistry; Amyloidogenic Proteins - chemistry; Atomic force microscopy; Biomaterials; Biomedical materials; Differential scanning calorimetry; Fibrillogenesis; Fluorescence; Hydration; Hydrophobic and Hydrophilic Interactions; Image analysis; Image processing; Imidazoles - chemistry; Ionic liquids; Ionic Liquids - chemistry; Ions; Kinetics; Lysozyme; Models, Molecular; Morphology; Muramidase - chemistry; Polymerization; Protein Aggregates; Protein Conformation; Protein Stability; Proteins; Solvents; Spectroscopy; Temperature; Thermal stability; Thermodynamics
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms23020783

Amyloid fibrils draw attention as potential novel biomaterials due to their high stability, strength, elasticity or resistance against degradation. Therefore, the controlled and fast fibrillization process is of great interest, which raises the demand for effective tools capable of regulating amyloid fibrillization. Ionic liquids (ILs) were identified as effective modulators of amyloid aggregation. The present work is focused on the study of the effect of 1-ethyl-3-methyl imidazolium-based ILs with kosmotropic anion acetate (EMIM-ac) and chaotropic cation tetrafluoroborate (EMIM-BF ) on the kinetics of lysozyme amyloid aggregation and morphology of formed fibrils using fluorescence and CD spectroscopy, differential scanning calorimetry, AFM with statistical image analysis and docking calculations. We have found that both ILs decrease the thermal stability of lysozyme and significantly accelerate amyloid fibrillization in a dose-dependent manner at concentrations of 0.5%, 1% and 5% ( / ) in conditions and time-frames when no fibrils are formed in ILs-free solvent. The effect of EMIM-BF is more prominent than EMIM-ac due to the different specific interactions of the anionic part with the protein surface. Although both ILs induced formation of amyloid fibrils with typical needle-like morphology, a higher variability of fibril morphology consisting of a different number of intertwining protofilaments was identified for EMIM-BF