TABLE 2.
Stabilizing effect of different surfactants on peptide α-helix
| Peptide | Surfactant | ΔXα (%) |
|---|---|---|
| Kn | β-C12G2 | 0 |
| (K4Y)n | β-C12G2 | 0 |
| (KY)n | β-C12G2 | ΔCD = 2.7 ± 0.1 mdeg* |
| (KY)n | α-C12G2 | ΔCD = 1.0 ± 0.1 mdeg* |
| (KF)n | β-C12G2 | 14.7 ± 0.3 |
| (KF)n | α-C12G2 | 11.3 ± 0.1 |
| (KF)n | β-C8G2 | 14.3 ± 0.6 |
| (KF)n | β-C10G2 | 15.1 ± 0.3 |
| (KF)n | β-C14G2 | 15.8 ± 0.1 |
| (KF)n | β-C7G1 | 22.4† |
| (KF)n | β-C8G1 | 22.9 ± 0.3 |
| (KF)n | β-C9G1 | 17.7 ± 0.8 |
| (KF)n | β-C12G3 | 12.5 ± 0.1 |
| (KF)n | C12E5 | 17.2 ± 0.8 |
| (KF)n | C12E6 | 16.7 ± 0.6 |
| (KF)n | C12E8 | 15.1 ± 0.4 |
The stabilizing effect is expressed as the increase in peptide α-helix fraction, ΔXα, at surfactant concentration ≥10 × CMC. The values represent the mean value from at least three independent measurements ± 1 SD. Standard deviations ≤0.1 are given as ±0.1.
*
For (KY)n, it is not possible to determine an absolute value for the increased amount of α-helix, due to inherent limitations of the CD technique (see Materials and Methods).
†
The (KF)n CMC required extremely large amounts of surfactant, and because of cost considerations, only one sample solution was prepared.