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. 2018 Aug 25;23(9):2142. doi: 10.3390/molecules23092142

Figure 2.

Figure 2

Atomic force (AFM) and electron microscope examination of aggregates of short sequences of hIAPP in its core mutation region. (A) AFM image24 (6 μm × 6 μm) of aged hIAPP23–27 (GAIL) in solution (10 mM). The vertical bar on the left-hand side of the figure indicates the heights of the measured objects. (B) Electron micrograph of insoluble aggregates of hIAPP23–27 (FGAIL) formed in an aged peptide solution. The apparent peptide concentration was 5.2 mg/mL in phosphate buffer (pH 7.4) with an incubation time of three days. The scale bar represents 200 nm. (C) Electron micrograph of insoluble aggregates of hIAPP22–27 (NFGAIL) formed in an aged peptide solution. The apparent peptide concentration was 6.4 mg/mL in phosphate buffer (pH 7.4) with an incubation time of three days. The scale bar represents 200 nm. Adapted from Tenidis et al. [30]. Copyright (2000) with permission from Elsevier.