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. Author manuscript; available in PMC: 2021 Feb 18.
Published in final edited form as: Biochemistry. 2020 Jan 30;59(6):742–754. doi: 10.1021/acs.biochem.9b01109

Figure 3.

Figure 3.

Double proline variants which contain an S28P substitution are significantly less amyloidogenic. (A) Time dependence of amyloid formation hIAPP and double proline variants in PBS. monitored by ThT fluorescence. hIAPP (black), IAPPA25P S28P (purple), IAPPA25P S29P (green), and IAPPS28P S29P (orange). (B) TEM images of hIAPP (black), IAPPA25P S28P (purple), IAPPA25P S29P (green), and IAPPS28P S29P (orange). Aliquots for TEM were collected at the conclusion of the ThT experiments. Assays were conducted using the following conditions: 16 μM peptide, 32 μM ThT, pH 7.4 10mM phosphate,140 mM KCl. 25°C. Scale bars in TEM images are 100 nm.