Acidic residue modifications restore chaperone activity of β-casein interacting with lysozyme
| Autor: | D Nourouzian, Ahmad Sharifzadeh, Ali Akbar Moosavi-Movahedi, Karim Zare, Nader Sheibani, Najmeh Poursasan, H. Hadi, H. Rajabzadeh, Mojtaba Amani, Faizan Ahmad |
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| Rok vydání: | 2011 |
| Předmět: |
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Molecular Protein aggregation Biochemistry Anilino Naphthalenesulfonates Fluorescence spectroscopy Accessible surface area chemistry.chemical_compound Structural Biology Animals Amino Acids Protein Structure Quaternary Molecular Biology Calorimetry Differential Scanning biology Caseins Isoxazoles General Medicine Dithiothreitol Spectrometry Fluorescence Sulfonate chemistry Chaperone (protein) Reagent biology.protein Cattle Muramidase Spectrophotometry Ultraviolet Target protein Lysozyme Chickens Protein Processing Post-Translational Molecular Chaperones Protein Binding |
| Zdroj: | International Journal of Biological Macromolecules. 49:616-621 |
| ISSN: | 0141-8130 |
| Popis: | An important factor in medicine and related industries is the use of chaperones to reduce protein aggregation. Here we show that chaperone ability is induced in β-casein by modification of its acidic residues using Woodward's Reagent K (WRK). Lysozyme at pH 7.2 was used as a target protein to study β-casein chaperone activities. The mechanism for chaperone activity of the modified β-casein was determined using UV–vis absorbencies, fluorescence spectroscopy, differential scanning calorimetry and theoretical calculations. Our results indicated that the β-casein destabilizes the lysozyme and increases its aggregation rate. However, WRK-ring sulfonate anion modifications enhanced the hydrophobicity of β-casein resulting in its altered net negative charge upon interactions with lysozyme. The reversible stability of lysozyme increased in the presence of WRK-modified β-casein, and hence its aggregation rate decreased. These results demonstrate the enhanced chaperone activity of modified β-casein and its protective effects on lysozyme refolding. |
| Databáze: | OpenAIRE |
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