Revealing the complexity of ionic liquid–protein interactions through a multi-technique investigation

Autor:	Karen M. Polizzi, Coby J. Clarke, Liem Bui-Le, Alex P. S. Brogan, Andreas Bröhl, James A. J. Arpino, Jason P. Hallett
Přispěvatelé:	Engineering & Physical Science Research Council (EPSRC)
Jazyk:	angličtina
Rok vydání:	2020
Předmět:	Circular dichroism 010405 organic chemistry Small-angle X-ray scattering Ionic bonding General Chemistry 010402 general chemistry 01 natural sciences Biochemistry 0104 chemical sciences Ion Protein–protein interaction lcsh:Chemistry chemistry.chemical_compound chemistry lcsh:QD1-999 Chemical physics Biocatalysis Ionic liquid Materials Chemistry Environmental Chemistry Trifluoromethanesulfonate
Zdroj:	Communications Chemistry, Vol 3, Iss 1, Pp 1-9 (2020)
ISSN:	2399-3669
DOI:	10.1038/s42004-020-0302-5
Popis:	Ionic liquids offer exciting possibilities for biocatalysis as solvent properties provide rare opportunities for customizable, energy-efficient bioprocessing. Unfortunately, proteins and enzymes are generally unstable in ionic liquids and several attempts have been made to explain why; however, a comprehensive understanding of the ionic liquid–protein interactions remains elusive. Here, we present an analytical framework (circular dichroism (CD), fluorescence, ultraviolet-visible (UV/Vis) and nuclear magnetic resonance (NMR) spectroscopies, and small-angle X-ray scattering (SAXS)) to probe the interactions, structure, and stability of a model protein (green fluorescent protein (GFP)) in a range (acetate, chloride, triflate) of pyrrolidinium and imidazolium salts. We demonstrate that measuring protein stability requires a similar holistic analytical framework, as opposed to single-technique assessments that provide misleading conclusions. We reveal information on site-specific ionic liquid–protein interactions, revealing that triflate (the least interacting anion) induces a contraction in the protein size that reduces the barrier to unfolding. Robust frameworks such as this are critical to advancing non-aqueous biocatalysis and avoiding pitfalls associated with single-technique investigations. Ionic liquids are used as solvents in biocatalysis but how they interact with the structures of proteins is imperfectly understood. Here the effect of three common ionic liquids on the structure of green fluorescent protein is studied using a suite of experimental techniques, finding a complex relationship which is poorly captured by any single technique.
Databáze:	OpenAIRE
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