Figure 3
From: A central role for dityrosine crosslinking of Amyloid-β in Alzheimer’s disease
Thioflavine T fluorescence and SDS PAGE of oxidized and control Aβ42. a) ThT fluorescence spectra following fibril formation from Aβ42 (20 μM) in the presence or absence of Cu2+ and H2O2 for 72 hours. The spectra for oxidized and control samples show an increased intensity over the incubation time and show increased ThT signal for non-oxidized compared to oxidized samples. b) SDS PAGE showing separation of Aβ42. Oxidized Aβ42 (left column) runs as monomer and dimer (approx. 9 kDa, black arrow), whilst non oxidized, control Aβ42 (right column) shows bands corresponding to monomer and trimer as previously observed [44]. The trimer is thought to be induced by SDS [44]. Densitometry confirms that monomer is the strongest band following by dimer for oxidized but not control fibrils. This reveals that the dimer is enriched under oxidation conditions.