Table 2.
Secondary structure analysis of the native and oxidized Aβ pentamer structures.
| System | β-sheet | β-bridge | Turn | Coil | α-, 3- and 5-helix |
|---|---|---|---|---|---|
| native | 73.3 | 2.1 | 9.7 | 14.9 | 0 |
| OX1 (3%) | 80.0 | 0.8 | 7.3 | 11.9 | 0 |
| OX2 (9%) | 74.7 | 0.8 | 8.7 | 15.8 | 0 |
| OX3 (15%) | 64.0 | 1.2 | 12.6 | 22.2 | 0 |
The values denote the relative occurrence (in %) of the various conformations.
Note that the hydrogen bonds between the chains are one of the factors that strengthen the inter-peptide interactions. Hence, a decrease in the number of hydrogen bonds results in weakening of the binding energy between the chains of Aβ pentamer.