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Related Experiment Video

Updated: Oct 25, 2025

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

Nonhuman IAPP Variants Inhibit Human IAPP Aggregation.

Alissa Oakes¹, Kate Menefee², Arleen Lamba¹

¹Department of Biology, Mount Saint Mary's University, Los Angeles, CA 90049, United States.

Protein and Peptide Letters

|August 9, 2021

Summary

Naturally occurring Islet Amyloid Polypeptide (IAPP) variants were identified that can inhibit toxic human IAPP aggregation. These findings offer potential therapeutic strategies for type 2 diabetes by protecting pancreatic beta cells.

Keywords:

Islet amyloid polypeptide amylin amyloid pancreas.protein aggregation type 2 diabetes

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Last Updated: Oct 25, 2025

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

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Published on: August 28, 2012

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System

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Published on: May 22, 2020

Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans

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Published on: November 26, 2017

Area of Science:

Biochemistry
Molecular Biology
Endocrinology

Background:

Type 2 diabetes progression is linked to toxic human Islet Amyloid Polypeptide (hIAPP) amyloid formation in the pancreas.
Loss of insulin-producing beta cells is associated with hIAPP aggregation.
Inhibiting hIAPP aggregation may slow or halt beta cell loss and disease progression.

Purpose of the Study:

To identify naturally occurring variants of IAPP.
To determine if these variants can inhibit human IAPP aggregation.
To assess their ability to protect living cells from toxic hIAPP effects.

Main Methods:

Synthetic hIAPP was incubated with naturally occurring IAPP variants.
Aggregation was assessed using Thioflavin T-binding fluorescence and atomic force microscopy.
Cell-rescue assays were performed to evaluate protective effects.

Main Results:

Most IAPP variants showed minimal inhibition of hIAPP aggregation.
Several variants demonstrated some inhibitory capacity.
Two specific variants exhibited substantial potential to inhibit hIAPP aggregation.

Conclusions:

Naturally occurring IAPP variants capable of inhibiting hIAPP aggregation were successfully identified.
These variants were characterized for their inhibitory potential.
The findings suggest these variants could be valuable in developing therapeutic interventions for type 2 diabetes.