Solvent induced changes in the conformational state of β-lactoglobulin and the influence of protic ionic liquids

Byrne, Nolene, Barrow, Colin and McCluskey, Adam 2012, Solvent induced changes in the conformational state of β-lactoglobulin and the influence of protic ionic liquids, Journal of molecular and engineering materials, vol. 1, no. 1, pp. 1-9.

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Title Solvent induced changes in the conformational state of β-lactoglobulin and the influence of protic ionic liquids
Author(s) Byrne, Nolene
Barrow, Colin
McCluskey, Adam
Journal name Journal of molecular and engineering materials
Volume number 1
Issue number 1
Start page 1
End page 9
Total pages 9
Publisher World Scientific Publishing
Place of publication Singapore
Publication date 2012
ISSN 2251-2373
2251-2381
Keyword(s) protic ionic liquids
β-lactogobulin
protein structure
β to α transition
amyloid fibril
Summary The protic ionic liquids (pILs), triethylammonium acetate, triethylammonium trifluoroacetate, triethylammonium mesylate and trimethylammonium sulfate were used to induce various native and non-native conformational states of the protein β-lactoglobulin (βLG). Changes in the secondary structure of βLG were observed on moving from a high water content to a high pIL content. We examined the stability of various pIL induced states via thermal unfolding and refolding, where it was found that at a given pIL concentration a highly stable non-native conformation was formed. The βLG non-native conformation was characterized by a high α-helical content. Additionally, pIL conditions that promoted amyloid fibril formation were identified and characterized by CD, a Thioflavin T binding assay and transmission electron microscopy (TEM). This work highlights the use of pILs as solvents in the study of protein folding using βLG as a model system.
Language eng
Field of Research 109999 Technology not elsewhere classified
Socio Economic Objective 970110 Expanding Knowledge in Technology
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2012, World Scientific Publishing
Persistent URL http://hdl.handle.net/10536/DRO/DU:30052660

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