Table 2. Degree of Peptide Helicity As Determined by Circular Dichroism.
| E3 |
K3 |
E3 + K3 |
||||
|---|---|---|---|---|---|---|
| anchor + spacer | θ222/θ208 | %Ha | θ222/θ208 | %Ha | θ222/θ208 | %Ha |
| acylb | 0.4 | 22 | 0.4 | 21 | 1.0 | 66 |
| CP0 | 0.9 | 16 | 0.8 | 79 | 0.8 | 52 |
| CP4 | 1.5 | 46 | 1.2 | 82 | 0.9 | 65 |
| CP8 | 0.9 | 52 | 1.0 | 60 | 1.2 | 71 |
| CP12 | 0.6 | 51 | 1.1 | 52 | 1.3 | 71 |
| CP16 | n.a.c | 7 | n.a.c | 28 | 1.3 | 48 |
| LP0 | 1.0 | 41 | 1.0 | 41 | 1.0 | 42 |
| LP2 | 1.1 | 33 | 1.0 | 43 | 1.1 | 40 |
| LP4 | 1.0 | 43 | 1.0 | 54 | 1.0 | 62 |
| LP8 | 0.9 | 37 | 1.0 | 63 | 1.1 | 62 |
| LP12 | 1.0 | 48 | 1.0 | 48 | 1.1 | 60 |
a
The percentage of α-helicity was calculated using the formula [θ]222 = −40 000(1 – 4.6/n) to obtain a 100% helicity value for an α-helical peptide of n residues.42
b
Measurements with acylated peptides, in PBS pH 7.4, without vesicles.
c
Negative ratio due to the positive θ208 value caused by a scattering artifact. [Total lipid] = 0.5 mM, with 1 mol % lipopeptides, PBS pH 7.4.