Four complexes of ß-hemocyanin from Helix pomatia (ß-HpH) with ionic liquids (ILs) based on cholinium cation and amino acid anion were prepared. Using FTIR spectroscopy we observed that the tested ILs were able to induce conformational changes in the protein molecule. In the presence of cholinium methionate we detected the most significant changes in ß-HpH secondary structure, which is expressed in a 2-fold increase of the intensity of the absorption band that is assigned to the side-chain

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... acid residues and a complete loss of the α-helical structures at expense of the ß-structures. Interestingly, the aggregation in this case seemed to be suppressed. In an experiment in vivo using 3T3 cells (fibroblasts), we found that the destabilization of the protein structure resulted in an enhanced cytotoxicity of the ß-HpH-IL complexes in respect to the native ß-HpH. The effect is stronger, both concentration-and time-dependent for the complex of ß-HpH with cholinium tryptophanate.