Table 1.
The sequences of P1, P2 and peptides modified based on P1 or P2.
| Name | Sequence | Net charge | MW (Da) | Modification description |
|---|---|---|---|---|
| P1 | FFKKF FKKFF KKFFK K-OH | +8 | 2220.84 | — |
| P1.1 | FFKKF FKKFF KKFF-OH | +6 | 1964.49 | C-ter truncate (2 amino acids) |
| P1.2 | FFKKF FKKFF KK-OH | +6 | 1670.14 | C-ter truncate (4 amino acids) |
| P1.3 | D-FFKKF FKKFF KKFFK K-OH | +8 | 2220.84 | D-amino acid substitution |
| P1.4 | FRKKF RKKFF KKFFK K-OH | +8 | 2238.82 | Sequence pattern, (FxKK)2(FFKK)2aa,b |
| P1.5 | FRKKF RKKFR KKFRK K-OH | +12 | 2256.85 | Sequence pattern, (FxKK)4 |
| P1.6 | FFKAF FKAFF KAFFK A-OH | +4 | 1992.45 | C-ter hydrophobic substitution and sequence pattern (FFKy)4ba,b |
| P2 | FFRRF FRRFF RRFFR R-OH | +8 | 2444.95 | — |
| P2.1 | EFRRE FRREF RREFR R-OH | 0 | 2372.70 | N-ter hydrophilic substitution and helical structure stabilization by E-R bridges |
| P2.2 | WYRRF YRRAH RRAHR R-OH | +8 | 2343.72 | N-ter hydrophobicity decreased & C-ter helical structure stabilization by AH |
| P2.3 | WYHHF YHHAH RRAHR R-OH | +4 | 2267.53 | N-ter hydrophobicity decreased and helical structure stabilization by AH, HH and WH bridge |
| P3 (negative control) | GTELP SPPSV WFEAE F-OH | −3 | 1792.99 | — |
a,b
x and y represent hydrophilic and hydrophobic amino acids, respectively.