Presentation Title

Human Islet Amyloid Polypeptide (IAPP) Aggregation is Inhibited in the Presence of IAPP of Alternate Species

Faculty Mentor

David Moffet

Start Date

17-11-2018 9:00 AM

End Date

17-11-2018 9:15 AM

Location

C161

Session

Oral 1

Type of Presentation

Oral Talk

Subject Area

biological_agricultural_sciences

Abstract

It is estimated that 30.3 million children and adults in the United States have type-II diabetes, approximately one out of every 10 individuals. Additionally, one in four adults living with the condition are unaware that they have the disease. These patients have been noted to lose pancreatic β-cells, with up to 45% loss of pancreatic mass in severe cases of the disease. It is believed that islet amyloid polypeptide (IAPP) is one of the agents responsible for the death of β-cells. This is because IAPP, for unknown reasons, accumulates in the pancreas, where it misfolds and subsequently aggregates into a variety of forms that are toxic to β-cells. Previous studies have been conducted that have enhanced the correlation between the aggregation of IAPP and the contraction of type II diabetes. In this research, we have shown that by selectively combining individual animal IAPP-variants, such as raccoon IAPP or dolphin IAPP, with human IAPP (hIAPP), the aggregation of hIAPP has been significantly reduced or inhibited. The findings of this work thus have the potential to be used as pharmaceutical therapeutics to treat patients with type-II diabetes.

Summary of research results to be presented

Data-collection methods include Atomic Force Microscopy (AFM), immunodot blot assays (Dot Blot), ELISA, and Thioflavin-T (Th-T) Assays. It is apparent from the results of these assays that hIAPP aggregation is inhibited in the presence of racoon IAPP and chicken IAPP. A 1:1 ratio of hIAPP to variant IAPP is sufficient to inhibit hIAPP aggregation. Interestingly, there is not a correlation between the ability of variant IAPP to inhibit hIAPP aggregation and amyloidogenicity of the variant IAPP itself. We believe this finding warrants further study.

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Nov 17th, 9:00 AM Nov 17th, 9:15 AM

Human Islet Amyloid Polypeptide (IAPP) Aggregation is Inhibited in the Presence of IAPP of Alternate Species

C161

It is estimated that 30.3 million children and adults in the United States have type-II diabetes, approximately one out of every 10 individuals. Additionally, one in four adults living with the condition are unaware that they have the disease. These patients have been noted to lose pancreatic β-cells, with up to 45% loss of pancreatic mass in severe cases of the disease. It is believed that islet amyloid polypeptide (IAPP) is one of the agents responsible for the death of β-cells. This is because IAPP, for unknown reasons, accumulates in the pancreas, where it misfolds and subsequently aggregates into a variety of forms that are toxic to β-cells. Previous studies have been conducted that have enhanced the correlation between the aggregation of IAPP and the contraction of type II diabetes. In this research, we have shown that by selectively combining individual animal IAPP-variants, such as raccoon IAPP or dolphin IAPP, with human IAPP (hIAPP), the aggregation of hIAPP has been significantly reduced or inhibited. The findings of this work thus have the potential to be used as pharmaceutical therapeutics to treat patients with type-II diabetes.