Neurodegenerative diseases such as Alzheimer’s disease (AD) and prion-related encephalopathies (PRE) are commonly identified by proteinaceous fibrillar aggregate deposits known as amyloids. Here we utilize a colorimetric, vesicle-binding assay to study protein-surface interactions of amyloid-forming proteins with lipid membranes. The assay consists of vesicles incorporated with polymerized polydiacetylene (PDA) molecules which provide a model system to mimic cell membranes. Lipid/PDA vesicles undergo a visible blue to red conversion in response to environmental conditions. From our spectroscopic data, we obtained time-resolved absorbance measurements of the “blue” (630 nm) and “red” (490 nm) components from lipid/PDA vesicles exposed to various amyloid-forming proteins such as β-amyloid (Aβ) and prion peptide fragments (PrP). Upon exposure to each amyloid-forming protein, we demonstrate the colorimetric responses of the lipid/PDA vesicles vary depending on the magnitude of protein association with the membrane. These studies illustrate the potential for this colorimetric assay to become a useful technique in studying biological systems.

Measuring amyloidogenic protein interaction with lipid membranes via colorimetric assay

249th National Meeting (2015)

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