Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 49, Issue 4, Pages 616-621Publisher
ELSEVIER
DOI: 10.1016/j.ijbiomac.2011.06.020
Keywords
Modified beta-casein; Lysozyme; Hydrophobicity; Woodward's Reagent K; Electrostatic potential; Accessible surface area
Funding
- Research Council of University of Tehran
- Iran National Science Foundation (INSF)
- Pasteur Institute of Iran
- IAU
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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 beta-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 beta-casein chaperone activities. The mechanism for chaperone activity of the modified beta-casein was determined using UV-vis absorbencies, fluorescence spectroscopy, differential scanning calorimetry and theoretical calculations. Our results indicated that the beta-casein destabilizes the lysozyme and increases its aggregation rate. However, WRK-ring sulfonate anion modifications enhanced the hydrophobicity of beta-casein resulting in its altered net negative charge upon interactions with lysozyme. The reversible stability of lysozyme increased in the presence of WRK-modified beta-casein, and hence its aggregation rate decreased. These results demonstrate the enhanced chaperone activity of modified beta-casein and its protective effects on lysozyme refolding. (C) 2011 Elsevier B.V. All rights reserved.
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