File(s) under permanent embargo
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 McCluskeyThe 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 materialsVolume
1Issue
1Pagination
1 - 9Publisher
World Scientific PublishingLocation
SingaporePublisher DOI
ISSN
2251-2373eISSN
2251-2381Language
engPublication classification
C1 Refereed article in a scholarly journalCopyright notice
2012, World Scientific PublishingUsage metrics
Categories
No categories selectedKeywords
protic ionic liquidsβ-lactogobulinprotein structureβ to α transitionamyloid fibrilScience & TechnologyTechnologyMaterials Science, MultidisciplinaryMaterials Sciencebeta-lactogobulinbeta to alpha transitionAMYLOID FIBRILSALPHA-HELIXPROTEINSTABILIZATIONPHTRIFLUOROETHANOLINTERMEDIATEAGGREGATIONIMPROVEMENT
Licence
Exports
RefWorks
BibTeX
Ref. manager
Endnote
DataCite
NLM
DC