Abstract
Amyloid β aggregation is an important factor in Alzheimer's disease. Since calcium homeostasis plays an important role in amyloid β aggregation, it is crucial to study the interaction between calcium ions and amyloid β directly at the surface of the lipid membrane. With supercritical angle techniques, the signal of interest at the surface is easily separated from the bulk solution, making them a powerful tool for aggregation study. In this work, the influence of calcium ions on amyloid β aggregation over different aggregation time periods is investigated with supercritical angle Raman and fluorescence spectroscopy and microscopy. Note that calcium ions have a larger influence on amyloid β(1-42) than on the 40 amino acid variant. We found that a small layer of calcium ions significantly protects the lipid membrane against the protein insertion process.