In recent studies it has been shown that individuals who have diabetes are at a higher predisposition of Alzheimer’s disease (AD). Insulin, which plays a large role in diabetes, is a peptide, similar in size to amyloid-beta (Aβ). Both of these peptides have a tendency to form aggregates due to their flexible secondary-structure assemblies. Despite this, there has been little to no research done on the aggregation patterns of Aβ and insulin and whether or not interactions between the two peptides is a cause for the close correlation between AD and diabetes. To study this interaction, Thioflavin T assays and gel electrophoresis were used to examine the aggregation patterns of these two biomolecules, both separately and mixed. Results from SDS-PAGE suggest that interactions between Aβ and insulin cause mixed aggregation to occur. More quantitative work is in progress to determine if the rates of these aggregates differ from the individual trials. In addition, recent findings indicate that it is the insulin B chain that causes high aggregation levels of insulin and that Aβ may play a role in the oxidation of the peptide into that form.<br/>

Aggregation mechanisms of amyloid-beta and insulin

253rd National Meeting (2017)

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