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. 2005 Jul 14;102(30):10427–10432. doi: 10.1073/pnas.0502066102

Fig. 2.

Fig. 2.

Electrophoresis of ABri, ADan, α-synuclein, amylin, SAA, and Aβ(1–40) on 16.5% SDS/PAGE under reducing conditions. The right lane shows peptide in aqueous solution; the left lane shows peptide in DOPC membrane after solubilization in 2% SDS. Positions of molecular mass markers are indicated on the left. Amylin and Aβ(1–40) were cross-linked both in solution and in membrane. In solution, for all peptides the monomers are observed. Small amounts of dimers are observed in solution for Aβ(1–40), ABri, and amylin. In the membrane, besides monomers and dimers, trimers are observed for amylin and Aβ(1–40), and tetramers are observed for ABri, amylin, Aβ(1–40), and α-synuclein. Also observed are pentamers for amylin and Aβ(1–40); hexamers for α-synuclein, SAA, ADan, amylin, and Aβ(1–40); and heptamers and octamers for α-synuclein and SAA.