Influence of alkyl chain substitution of ammonium ionic liquids on the activity and stability of tobacco etch virus protease

Ionic liquids (ILs) are known to provide stability to biomolecules. ILs are also widely used in the fields of chemical engineering, biological engineering, chemistry, and biochemistry because they facilitate enzyme catalyzed reactions and enhance their conversion rate. In this work, we have evaluate...

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Bibliographic Details
Published in:International journal of biological macromolecules 2020-07, Vol.155, p.439-446
Main Authors: Attri, Pankaj, Choi, Sooho, Kim, Minsup, Shiratani, Masaharu, Cho, Art E., Lee, Weontae
Format: Article
Language:English
Subjects:
Ammonium Compounds - chemistry
Endopeptidases - chemistry
Endopeptidases - metabolism
Enzyme Stability
Ionic liquids
Ionic Liquids - chemistry
Models, Molecular
Molecular Dynamics Simulation
Molecular dynamics simulations
Protein Conformation
Solvents - chemistry
Tobacco etch virus protease
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Summary:Ionic liquids (ILs) are known to provide stability to biomolecules. ILs are also widely used in the fields of chemical engineering, biological engineering, chemistry, and biochemistry because they facilitate enzyme catalyzed reactions and enhance their conversion rate. In this work, we have evaluated the influence of alkyl chain substitution of ammonium ILs such as diethylammonium dihydrogen phosphate (DEAP) and triethylammonium hydrogen phosphate (TEAP) for the stability and activity of the tobacco etch virus (TEV) protease. Further, we performed molecular dynamics (MD) simulations to calculate the RMSD (root mean square deviation) for TEV and TEV + ILs. Experimental and simulations results show that TEV is more stable in the presence of TEAP than DEAP. Whereas, TEV protease activity for the cleavage of fusion proteins is preserved in the presence of DEAP while lost in the presence of TEAP. Hence, DEAP IL can serve as alternative solvents for the stability of the TEV protease with preserved activity. To the best of our knowledge, this is first study to show that ILs can stabilize and maintain the TEV protease cleavage activity.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2020.03.175