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Cholinium-Based Ionic Liquids Modulate Protein Stability: A Comparative Study of Enzymes and Albumins
Artashes A Khachatrian1, Timur A Mukhametzyanov1, Ramazan Z Salikhov1
1Department of Physical Chemistry, Kazan Federal University, Kremlyovskaya 18, Kazan 420008, Russia.
Molecules (Basel, Switzerland)
|April 26, 2025
Summary
Choline ionic liquids interact with enzymes like lysozyme and α-chymotrypsin. While binding is similar to albumins, these ionic liquids oppositely affect enzyme thermostability and promote aggregation more in albumins.
Area of Science:
- Biochemistry
- Chemical Biology
- Protein Science
Background:
- Ionic liquids (ILs) are versatile solvents with tunable properties.
- Understanding IL-protein interactions is crucial for applications in biotechnology and drug delivery.
- Choline-based ILs are explored for their potential biocompatibility.
Purpose of the Study:
- To investigate the intermolecular interactions between specific choline ionic liquids (choline malonate, choline succinate, choline valinate) and two model enzymes (lysozyme, α-chymotrypsin).
- To evaluate the impact of these ILs on enzyme structure, stability, and aggregation.
- To compare the behavior of enzymes in IL solutions with previously studied albumins.
Main Methods:
- Circular dichroism (CD) spectrometry to assess tertiary protein structure changes.
- Fluorescence spectroscopy to quantify IL-enzyme binding parameters.
- Molecular docking to estimate binding energies and ion localization on enzymes.
- Thermostability and aggregation assays for enzyme/IL systems.
Main Results:
- Choline ionic liquids bind to lysozyme and α-chymotrypsin with comparable binding constants.
- ILs demonstrated opposite effects on enzyme thermostability compared to their effects on albumins.
- Ionic liquids induced protein aggregation in both enzymes and albumins, with a more pronounced effect on albumins.
Conclusions:
- Choline ionic liquids exhibit distinct interactions with enzymes versus albumins, particularly concerning thermostability.
- The aggregation propensity induced by ILs is significantly higher in albumins than in enzymes.
- These findings highlight the nuanced effects of ionic liquids on different protein classes, informing their application design.
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