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

journal contribution
posted on 2012-01-01, 00:00 authored by Nolene ByrneNolene Byrne, Colin BarrowColin Barrow, A McCluskey
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.

History

Journal

Journal of molecular and engineering materials

Volume

1

Issue

1

Pagination

1 - 9

Publisher

World Scientific Publishing

Location

Singapore

ISSN

2251-2373

eISSN

2251-2381

Language

eng

Publication classification

C1 Refereed article in a scholarly journal

Copyright notice

2012, World Scientific Publishing