Double-edged effects of aluminium ions on amyloid fibrillation of hen egg-white lysozyme.

Elucidating the effects of Al(III) ions on amyloid fibrillation is important to understand the association between metal ions and Alzheimer's disease. Here, Raman spectroscopy was applied to investigate amyloid fibrillation of hen egg-white lysozymes during thermal incubation with Al(III) ions or acids, combined with atomic force microscopy and thioflavin T fluorescence assays. Kinetics of conformational changes in lysozymes were assessed by monitoring six characteristic Raman spectral markers. The peak of Phe residues at 1003 cm and two bands of Trp residues at 759 cm and 1340-1360 cm corresponded to the lysozyme tertiary structure, whereas two NCC stretching vibrations at 899 cm and 935 cm and an amide I band were associated with the lysozyme skeleton. There may be a four-stage transformation mechanism underlying the kinetics of amyloid fibrillation of lysozymes with the thermal/Al(III) treatment. Comparison of kinetics under thermal/Al(III) and thermal/acid conditions revealed double-edged roles of Al(III) ions in amyloid fibrillation of lysozymes. Specifically, in addition to postponing α-helix degradation, Al(III) ions accelerated conformational transformations from α-helices to organized β-sheets. The present investigation sheds light on the controversial effects of Al(III) ions on amyloid fibrillation of lysozymes.