Zn(II), Cu(II), Sn(II), and Ni(II) and other metal cations do not prevent the aggregation of hIAPP

Author

Charles HoyingFollow

Date of Completion

5-5-2016

Degree Type

Honors Thesis

Discipline

Chemistry (CHEM)

First Advisor

David Moffet

Abstract

The Zn(II) metal ion has been shown to interact with Islet Amyloid Polypeptide (IAPP), a protein implicated in the progression of Type II Diabetes Mellitus, in such a way as to prevent the protein from aggregating into toxic fibers. We set out to find whether other metal ions might similarly prevent IAPP aggregation. Using Thioflavin T (ThT) spectroscopic assays, which measure fluorescence of ThT upon binding to aggregated IAPP, we observed a decrease in aggregation when incubated with Zn(II), Cu(II), Ni(II), and Sn(II). Atomic Force Microscopy (AFM), which can visualize fibril formation, revealed that the metals were not inhibiting IAPP aggregation. Instead, the metals may have promoted fibril formation at the concentrations tested, which may be too high; it has been proposed that separate mechanisms exist at low and high metal concentrations inhibiting or promoting IAPP aggregation. Therefore, further research should optimize inhibitory concentration for the metals tested in this study.

Recommended Citation

Hoying, Charles, "Zn(II), Cu(II), Sn(II), and Ni(II) and other metal cations do not prevent the aggregation of hIAPP" (2016). Honors Thesis. 118.
https://digitalcommons.lmu.edu/honors-thesis/118