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Incubation of Aβ1–40 fibrils with RNase A destabilized by reducing agent leads to loss of ThT fluorescence. Aβ1–40 fibrils (preaggregated from 20 µM monomerized Aβ1–40) were incubated with PBS or 3 µM RNase A ± 5 mM β-mercaptoethanol (BME). Only RNase A + BME (grey), which reduces its disulfide bonds to destabilize the protein, leads to loss of fibril ThT fluorescence.
