Although Alzheimer’s and COVID-19 are different diseases, the commonality between them is during the process of them developing in a person by fibrillogenesis. The product of fibrillogenesis results in the development of these diseases. We study the first stage of fibrillogenesis where the amyloid-beta peptide monomers are assembled into an oligomer. We want to isolate this oligomer using gold colloids because this step can be reversed. Utilizing gold colloids allows us to freeze fibrillogenesis in the first step by folding and unfolding the protein repeatedly through a series of pH changes from 4 or below to 10 or higher. At an acidic state (pH~4), the protein is unfolded and aggregates while during a basic state (pH~10), the protein is folded and dispersed. A UV-vis spectrophotometer is used to view the results of the change in acidic to basic conditions. For our research we try to keep the amyloid-beta protein in a quasi-reversible state, so we are able to continue to switch between a pH of 4 and 10 to better observe the protein structures of Alzheimer’s and COVID-19.
Spencer, Renee; Kocieniewski, Lila; Martinez, Bryan; and Yokoyama, Kazushige, "Amyloid-Beta Protein Concentration Dependence of Reversible Aggregation Using Gold Colloid Particles" (2023). McNair Scholars Program. 13.