Table 4. Composition of the peptide secondary structures as determined by ATR-FTIR spectroscopy from the deconvolution of the amide I bands of the peptides incorporated into the lipid multibilayers.
A 30:1 lipid/peptide molar ratio was used. cho, cholesterol; erg, ergosterol.
| Peptide | Lipid composition | Helical structure* (%) | β-Sheet structure† (%) | Random coil (%) |
|---|---|---|---|---|
| [D]-L6K6 | PC/cho | 57 | 43 | – |
| PE/PG | 54 | 46 | – | |
| PE/PC/PI/erg | 45 | 25 | 30 | |
| [D]-L6K6-DA | PC/cho | 62 | 38 | – |
| PE/PG | 47 | 53 | – | |
| PE/PC/PI/erg | 45 | 28 | 27 | |
| [D]-L6K6-DDA | PC/cho | 70 | 30 | – |
| PE/PG | 58 | 42 | – | |
| PE/PC/PI/erg | 46 | 29 | 25 | |
| [D]-L6K6-MA | PC/cho | 64 | 36 | – |
| PE/PG | 58 | 42 | – | |
| PE/PC/PI/erg | 53 | 47 | – | |
| [D]-L6K6-PA | PC/cho | 78 | 22 | – |
| PE/PG | 65 | 35 | – | |
| PE/PC/PI/erg | 53 | 47 | – |
* The sum of both α-helical and 310-helix/dynamic helix regions.
† β-Sheet structure refers to both low-frequency β-sheet and high-frequency β-turns component regions.