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Full-Text Articles in Inorganic Chemicals
Zn(Ii), Cu(Ii), Sn(Ii), And Ni(Ii) And Other Metal Cations Do Not Prevent The Aggregation Of Hiapp, Charles Hoying
Zn(Ii), Cu(Ii), Sn(Ii), And Ni(Ii) And Other Metal Cations Do Not Prevent The Aggregation Of Hiapp, Charles Hoying
Honors Thesis
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 …
Investigating Metal Cations As Potential Inhibitors Of Iapp Aggregation: Kcl, Cacl2, And Cucl2, Megan Burke
Investigating Metal Cations As Potential Inhibitors Of Iapp Aggregation: Kcl, Cacl2, And Cucl2, Megan Burke
Honors Thesis
IAPP is an amyloid protein that misfolds, causing toxic aggregation in the pancreas of Type II Diabetes patients. In this study, three metal cations (KCl, CaCl2, and CuCl2) are tested in Thioflavin T assays and atomic force microscopy (AFM) to see if they inhibit the aggregation of IAPP.