A common feature among various neurological disorders is the misfolding of protein/peptide, which is typically followed by aggregation/fibrillation and deposition of aggregates onto neuronal membranes. In this presentation, we will describe the use of surface plasmon resonance (SPR) spectroscopy for the study of oligomerization/fibrillation of amyloid beta (Aβ) peptides at lipid bilayers, an event believed to lead to Alzheimer’s disease. We will also discuss the effects of metal ions on the aggregation of α-synuclein, which is a key step in the development of Parkinson’s disease. We will also describe the use of related biophysical techniques such as circular dichroism and chromatography for investigating the inhibition of amyloidogenisis of these pepetides/proteins by natural small molecules. Finally, we will present our recent data on the use of SPR microscopy for real-time monitoring of the initial binding and subsequent aggregation of Aβ peptides at single neuroblastoma cells.

Surface plasmon resonance and related biophysical techniques for the studies of amyloid peptide and protein aggregation and the Inhibition of aggregation by natural products

256th National Meeting (2018)

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