Table 2. Secondary structure content of aS dimers fibrils as determined by FTIR spectroscopy reported in Fig. 6 and in Fig. S5.
Wavenumber a (cm−1) | Structural Assignment | aS % b | NN % b | CC % b | NC % b | DC % b |
1560–1568 | Glu (COO−) | 23 | 33 | 48 | 3 | 8 |
1580–1586 | Asp (COO−) | 5 | - | - | 3 | 4 |
1612–1619 | Aggregated β-sheet | 31 | 18 | 13 | 32 | 46 |
1634–1636 | β-sheet | 18 | - | 18 | - | - |
1640–1650 | Random | - | 33 | 11 | 38 | 16 |
1656–1668 | Turns | 19 | 15 | 9 | 22 | 24 |
1680–1689 | Anti-parallel aggregated β-sheet | 4 | 1 | 1 | 2 | 2 |
Peak position of the amide I band components, as deduced by the second derivative spectra.
Percentage area of the amide I band components, as obtained by integrating the area under each deconvoluted band. The areas corresponding to side chain contributions located at 1700–1710 cm−1 have not been considered.