New insight into the alcohol induced conformational change and aggregation of the alkaline unfolded state of bovine β-lactoglobulin
Autor: | Hasan Parvej, Sampa Pal, Umesh Ch. Halder, Subrata Sardar, Sanhita Maity, Jishnu Chakraborty |
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Rok vydání: | 2016 |
Předmět: |
Conformational change
General Chemical Engineering Intermolecular force Alcohol 02 engineering and technology General Chemistry Protein aggregation 010402 general chemistry 021001 nanoscience & nanotechnology Fibril 01 natural sciences Protein tertiary structure 0104 chemical sciences Folding (chemistry) chemistry.chemical_compound chemistry Biophysics Organic chemistry Methanol 0210 nano-technology |
Zdroj: | RSC Advances. 6:74409-74417 |
ISSN: | 2046-2069 |
Popis: | Accumulation of ordered protein aggregates (or amyloids) is responsible for several neurodegenerative diseases. β-Lactoglobulin (β-lg) an important globular milk protein, self-assembles to form amyloid-like fibrils on heating at low pH. But here we report for first time the self-assembly of β-lg from its alkaline unfolded state. The present work describes the folding and self-assembly of β-lg from a reversible unfolded state at pH 10.5 in the presence of methanol, 2-propanol, t-butanol and 2,2,2-trifluoroethanol (TFE). The extent of secondary and tertiary structure formation is in the order methanol < 2-propanol < t-butanol < TFE. Exposure of the hydrophobic core of the protein molecules in an apolar environment of TFE seems to promote intermolecular cluster formation. Methanol and TFE induce aggregation through the α-helical structure whereas isopropanol and t-butanol favour the formation of the β-structure leading to aggregation at higher concentrations. In vitro aggregation generates various nanometer structures such as nanofibrils, nanovesicles and nanotubes depending on the nature and concentration of the alcohols. |
Databáze: | OpenAIRE |
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