Table 1.
Peptide | Sequence | (H)1 | (H)2 | (μH)1* |
---|---|---|---|---|
D-LAK120 | KKLALLALKKWLLALKKLALLALKK-NH2 | 1.26 | −0.05 | 1.28 |
D-LAK120-P13 | KKLALLALKKWLPALKKLALLALKK-NH2 | 0.87 | −0.07 | 1.66 |
D-LAK120-A | KKLALALAKKWLALAKKLALALAKK-NH2 | −0.02 | −0.08 | 2.28 |
D-LAK120-AP13 | KKLALALAKKWLPLAKKLALALAKK-NH2 | 0.00 | −0.10 | 2.25 |
D-LAK120-H | KKLALHALKKWLHALKKLAHLALKK-NH2 | −0.35 | −0.16 | 2.80 |
D-LAK120-HP13 | KKALAHALKKWLPALKKLAHALAKK-NH2 | −1.07 | −0.17 | 3.81 |
D-LAK80-HP13 | KKALAKALKHWLPALHKLAKALAKK-NH2 | −1.07 | −0.17 | 4.02 |
D-LAK160-HP13 | KKALKHALAKWLPALKALAHKLAKK-NH2 | −1.07 | −0.17 | 3.40 |
LAK80 | KKLAKALKLLALLWLKLAKALKKA-NH2 | 0.46 | −0.09 | 3.73 |
LAK80-P7 | KKLAKAPKLLALLWLKLAKALKKA-NH2 | 0.05 | −0.11 | 3.46 |
LAK80-P10 | KKLAKALKLPALLWLKLAKALKKA-NH2 | 0.05 | −0.11 | 3.33 |
LAK80-P12 | KKLAKALKLLAPLWLKLAKALKKA-NH2 | 0.05 | −0.11 | 4.14 |
LAK120 | KKLALALKKLALLWKKLALALKKA-NH2 | 0.46 | −0.09 | 3.02 |
LAK120-P7 | KKLALAPKKLALLWKKLALALKKA-NH2 | 0.05 | −0.11 | 2.76 |
LAK120-P10 | KKLALALKKPALLWKKLALALKKA-NH2 | 0.05 | −0.11 | 2.62 |
LAK120-P12 | KKLALALKKLAPLWKKLALALKKA-NH2 | 0.05 | −0.11 | 3.43 |
LAK160 | KKLKLALAKLALLWKALALKLKKA-NH2 | 0.46 | −0.09 | 2.59 |
LAK160-P7 | KKLKLAPAKLALLWKALALKLKKA-NH2 | 0.05 | −0.11 | 2.34 |
LAK160-P10 | KKLKLALAKPALLWKALALKLKKA-NH2 | 0.05 | −0.11 | 2.18 |
LAK160-P12 | KKLKLALAKLAPLWKALALKLKKA-NH2 | 0.05 | −0.11 | 3.00 |
LAK80-F1 | FKKLAKALKLLALLALKLAKALKKA-NH2 | 0.41 | −0.06 | 3.36 |
LAK80-F2 | FFKKLAKALKLLALLALKLAKALKKA-NH2 | 0.78 | −0.04 | 3.55 |
LAK80-F2-P9 | FFKKLAKAPKLLALLALKLAKALKKA-NH2 | 0.40 | −0.06 | 3.30 |
Comparison of physical features of peptides used in this study. Hydrophobicity (H) and mean hydrophobic moment (μH) are shown according to the Combined Consensus scale1 or Eisenberg scale2 and were calculated using the HydroMCalc Java applet made available by Alex Tossi (http://www.bbcm.univ.trieste.it/~tossi/HydroCalc/HydroMCalc.html). All peptides contain eight lysine residues and are amidated at the C-terminus conferring a nominal charge of +9 at neutral pH.
Mean hydrophobic moment assuming formation of ideal α-helix.