The role of metal ions in the fibrillization of lysozyme and insulin in vitro
Keywords:
amyloid fibrils, insulin, lysozyme, metal ions, Thioflavin TAbstract
The effects of metal ions on the fibrillization of lysozyme and insulin were investigated using a
Thioflavin T fluorescence assay and transmission electron microscopy. The incubation of the proteins in
acidic buffer at high temperature in the presence of substoichiometric concentrations of Сu2+, Zn2+, Fe3+
and Al3+ primarily led to the decrease in lag phase of fibril growth and protein aggregation rate compared to those in control samples. Furthermore, Сu2+ and Fe3+ showed a stronger influence on the protein fibrillization than Zn2+ and Al3+. Specifically, Сu2+ and Fe3+ provoked the formation of insulin amyloid fibrils, having a «fuzzy» appearance, while the amyloid-like insulin aggregates grew in the presence of Zn2+. These results highlight the potential of metal ions as prospective therapeutic agents against human«conformational» diseases.
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