Stabilization of Haloalkane Dehalogenase Structure by Interfacial Interaction with Ionic Liquids
| Autoři | |
|---|---|
| Rok publikování | 2021 |
| Druh | Článek v odborném periodiku |
| Časopis / Zdroj | Crystals |
| Fakulta / Pracoviště MU | |
| Citace | |
| www | https://www.mdpi.com/2073-4352/11/9/1052 |
| Doi | http://dx.doi.org/10.3390/cryst11091052 |
| Klíčová slova | haloalkane dehalogenase (HLD); ionic liquids (ILs); molecular dynamics (MD) simulations; protein stability; 2-hydroxyethylammonium acetate ([ETA][ACC]); 1-butyl-3-methylimidazolium methyl sulfate ([EMIM][CHS]) |
| Přiložené soubory | |
| Popis | Ionic liquids attracted interest as green alternatives to replace conventional organic solvents in protein stability studies. They can play an important role in the stabilization of enzymes such as haloalkane dehalogenases that are used for biodegradation of warfare agents and halogenated environmental pollutants. Three-dimensional crystals of haloalkane dehalogenase variant DhaA80 (T148L+G171Q+A172V+C176F) from Rhodococcus rhodochrous NCIMB 13064 were grown and soaked with the solutions of 2-hydroxyethylammonium acetate and 1-butyl-3-methylimidazolium methyl sulfate. The objective was to study the structural basis of the interactions between the ionic liquids and the protein. The diffraction data were collected for the 1.25 angstrom resolution for 2-hydroxyethylammonium acetate and 1.75 angstrom resolution for 1-butyl-3-methylimidazolium methyl sulfate. The structures were used for molecular dynamics simulations to study the interactions of DhaA80 with the ionic liquids. The findings provide coherent evidence that ionic liquids strengthen both the secondary and tertiary protein structure due to extensive hydrogen bond interactions. |
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