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. 2012 Nov 15;109(49):19965–19970. doi: 10.1073/pnas.1208797109

Fig. 7.

Fig. 7.

IAPP and α-Synuclein gammabodies potently inhibit amyloid formation in a sequence-specific manner. IAPP (32 μM) and α-Synuclein (residues 1–115, 50 μM) were incubated in the absence (control) and presence of gammabodies (1:10 gammabody:monomer molar ratio), and fibrillization was monitored via (A) immunoblotting and (B) AFM. In B, IAPP and α-Synuclein fibrillization was also monitored in the presence of sequence-specific (R10/99, IAPP residues 7–17; 5C2, α-Synuclein residues 61–95) and conformation-specific (A11, prefibrillar oligomers; OC, fibrillar conformers) antibodies (1:10 antibody:monomer molar ratio). In B, the AFM images are 3 × 3 μm, and the blank images are samples with heights <1 nm. The heights of the IAPP and α-Synuclein aggregates are 21 ± 3 and 25 ± 4 nm, respectively.