TABLE 1.
Amino acid sequences and α‐helix content of human apolipoprotein A1 (apoA‐I) fragments and apoA‐I mimetic peptides.
| α‐helix content, % | |||
|---|---|---|---|
| Peptide | Sequence | in H2O | in 50%TFE |
| apoA‐I221–240 | H‐VLESFKVSFLSALEEYTKKL‐OH | 18.97 | 46.62 |
| P1 |
|
10.11 | 65.87 |
| P2 |
|
8.15 | 59.60 |
| P3 |
|
7.11 | 61.11 |
| P4 |
|
6.87 | 59.25 |
| P5 |
|
5.67 | 67.23 |
| P6 |
|
‐0.41 | 72.80 |
| P7 |
|
3.55 | 68.64 |
| P8 |
|
9.71 | 61.36 |
| P9 |
|
9.24 | 61.45 |
| P10 |
|
17.42 | 63.11 |
| P11 |
|
59.23 | 63.85 |
| P12 |
|
70.23 | 62.34 |
| P13 |
|
75.16 | 91.96 |
| P14 |
|
75.84 | 74.80 |
| P15 |
|
30.27 | 42.62 |
| P16 |
|
40.01 | 15.36 |
| P17 |
|
30.78 | 16.41 |
| L‐4F a | Ac‐DWFKAFYDKVAEKFKEAF‐NH2 | 52.77 | 66.25 |
a
L‐4F was used as a positive control. The amino acids that were substituted in the parent peptide apoA‐I221–240, are shown in bold. The letters in the box represent the unchanged amino acid residues of the hydrophilic face. apoA‐I, apolipoprotein A1; TFE, trifluoroethanol.