Stabilization of Haloalkane Dehalogenase Structure by Interfacial Interaction with Ionic Liquids

Authors

Shaposhnikova, A., Kuty, M., Chaloupkova, R., Damborsky, J., Kuta Smatanova, I., Minofar, B., Prudnikova, T.

Source

CRYSTALS 11: 1052 (2021)

Abstract

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 Å resolution for 2-hydroxyethylammonium acetate and 1.75 Å 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. 

Full text

Citation

Shaposhnikova, A., Kuty, M., Chaloupkova, R., Damborsky, J., Kuta Smatanova, I., Minofar, B., Prudnikova, T., 2021: Stabilization of Haloalkane Dehalogenase Structure by Interfacial Interaction with Ionic Liquids. Crystals 11: 1052.

David Awarded by MUNI Scientist Award
Tonda Succesfully Defended Doctoral Thesis
LL & Enantis Awarded by MUNI Innovation Award
Lucia’s Success at AMAVET Competition
Ph.D. Student Wanted
Martin Selected for Global Young Scientists Summit
Honza to Present at 17th P4EU Meeting