Khachatrian Artashes A, Mukhametzyanov Timur A, Salikhov Ramazan Z, Klimova Alexandra E, Yakhvarov Dmitry G, Garifullin Bulat F, Terenteva Olga S, Padnya Pavel L, Stoikov Ivan I, Solomonov Boris N
Department of Physical Chemistry, Kazan Federal University, Kremlyovskaya 18, Kazan 420008, Russia.
Arbuzov Institute of Organic and Physical Chemistry, FRC Kazan Scientific Center of RAS, Arbuzov St. 8, Kazan 420008, Russia.
Molecules. 2025 Mar 31;30(7):1574. doi: 10.3390/molecules30071574.
This work aims to assess the intermolecular interaction of choline ionic liquids (ILs) (choline malonate ([Ch][Mal]), choline succinate ([Ch][Suc]), and choline valinate ([Ch][Val]) with two enzymes (lysozyme and α-chymotrypsin). We evaluated the state of the tertiary protein structure using circular dichroism (CD) spectrometry and quantified the binding parameters of the binding of the ionic liquids to the enzymes by fluorescence spectroscopy. The binding energies of the enzymes and the localization of ions on them were estimated using the molecular docking. We then analyzed the relationship between the enzymes' thermostability and their tendency towards aggregation in the enzyme/ionic liquid systems. The obtained results were compared with previous data on albumins to identify similarities and differences between the behavior of enzymes and albumins in ionic liquid solutions. Despite the comparable values of the binding constants, the effect of ionic liquids on the thermostability of enzymes was the opposite of their effect on albumins. In addition, although these ionic liquids promoted aggregation in both enzymes and albumins, this effect was much more pronounced for albumins.
这项工作旨在评估胆碱离子液体（ILs）（丙二酸胆碱([Ch][Mal])、琥珀酸胆碱([Ch][Suc])和缬氨酸胆碱([Ch][Val])）与两种酶（溶菌酶和α-胰凝乳蛋白酶）之间的分子间相互作用。我们使用圆二色性（CD）光谱法评估三级蛋白质结构的状态，并通过荧光光谱法定量离子液体与酶结合的结合参数。利用分子对接估计酶的结合能及其上离子的定位。然后，我们分析了酶/离子液体系统中酶的热稳定性与其聚集倾向之间的关系。将所得结果与先前关于白蛋白的数据进行比较，以确定酶和白蛋白在离子液体溶液中行为的异同。尽管结合常数的值相当，但离子液体对酶热稳定性的影响与其对白蛋白的影响相反。此外，虽然这些离子液体促进了酶和白蛋白的聚集，但这种效应在白蛋白中更为明显。
