Mass spectra of 20 μM Aβ40 peptide dissolved in 20 mM ammonium acetate buffer, pH 7.4, with and without addition of toluene and Pb(IV) acetate at 1:1 ratios were recorded three times each on a Synapt G2-Si high definition mass spectrometer (Waters corporation) equipped with a conventional ESI source operating in positive ion mode. Flow rate was 20 μl/min, capillary voltage 2.5 kV, cone voltage 40 V. Analysis was done in high-resolution mode (average resolution of 30 000) in the 500–4000 m/z range.
Data processing was done using the Proteowizard124 (link), UniDec125 (link), and mMass126 (link) softwares. Peaks were identified by comparison between raw experimental data and generated theoretical peak lists, and by analysis of isotopic patterns (Supp. Fig.S4 ). All data were normalized to the +4 charge state signal of the Aβ monomer, to account for small deviations in concentration and ionization efficacy across samples.
Data processing was done using the Proteowizard124 (link), UniDec125 (link), and mMass126 (link) softwares. Peaks were identified by comparison between raw experimental data and generated theoretical peak lists, and by analysis of isotopic patterns (Supp. Fig.
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