egg-white and Protein-Aggregation--Pathological

In vitro fibrillation of hen egg white lysozyme (HEWL) causes complete reduction of Cu(II) to Cu(I) at pH 7. Here in the present article, we have shown the presence of both Cu(II) and Cu(I) at pH 11 during fibrillation of HEWL using electron paramagnetic resonance and Raman spectroscopy. Our results suggest the existence of a partially reducing environment during fibrillation of hen egg white lysozyme at pH 11. The fibrillation process is governed by the pH of the solution and maximum fibrillation is found to occur at pH 11. Fibrils formed in the absence of Cu(II) were also found to cause significant hemolysis of RBC.

Topics: Amyloid; Animals; Copper; Egg White; Female; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Muramidase; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Protein Aggregates; Protein Aggregation, Pathological; Protein Conformation; Protein Multimerization; Spectrum Analysis, Raman