Journal
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
Volume 214, Issue -, Pages 239-245Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2019.02.032
Keywords
Lysozyme; Ionic liquids; Binding domains; Spectroscopic studies
Categories
Funding
- National Natural Science Foundation of China [21676196]
- Tianjin Municipal Natural Science Foundation [17JCYBJC20400]
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The binding domains of lysozyme with ionic liquids (ILs, [C(4)mim]BF4, [C(4)mim]Cl, [C(4)mim]Br and [dmim]I) in aqueous solution was investigated by studying molecular interactions using spectroscopic techniques. Ultraviolet spectroscopy (UV) showed that the addition of ILs increased the absorption peak intensity of lysozyme at 210 nm by enhancing peptide bond valence electron transition. It is also found that a weak interaction between ILs and lysozyme chromophore groups was generated by analyzing the changes of absorption peak intensity near 280 nm. Fluorescence and Synchronous Fluorescence spectra results showed that four ILs had quenching effect on the fluorescent substances of lysozyme, and the quenching effect rose with increasing ILs concentration. Meanwhile, the interaction between lysozyme and ILs molecules is mainly based on Van der Waals force and two Tryptophan (Trp) residues (Trp62 or Trp108) at the active site of lysozyme molecules play a critical role in binding ILs to their own molecules. (C) 2019 Published by Elsevier B.V.
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