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. 2022 Oct 28;12(11):1585. doi: 10.3390/biom12111585

Figure 3.

Figure 3

(a) ThT fluorescence emission intensity monitored as a function of time. Copper (one equivalent, as CuCl2) was added at time 0 min after previously allowing NKB (▲), NKB(H3F) (■), and NKB(H3W) (►) to aggregate in 10 mM nEM, pH 7.8 buffer. Copper can disassemble wildtype NKB faster than either NKB(H3F) or NKB(H3W). However, copper delivered as a glycine complex ([Cu(gly)2]) leads to rapid disassembly of NKB(H3F) (●) after aggregation in 10 mM nEM. Dashed lines represent the standard deviation of the NKB(H3W) measurement (n = 3) and are representative of the variation in all measurements. (b) Mass spectrum obtained after copper addition to NKB(H3W) shows peaks due to metal-free peptide (m/z 1259.4) and to metal-bound peptide (m/z 1320.4). (c) Mass spectrum obtained after copper addition to NKB(H3F) shows peaks due to metal-free peptide (m/z 1220.5) and to metal-bound peptide (m/z 1281.4). In both panels (b,c), the inset highlights the peak manifolds corresponding to copper-bound peptides with the simulated spectrum (red dotted line) assuming one copper ion is bound to the peptide.