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. Author manuscript; available in PMC: 2012 Oct 9.
Published in final edited form as: J Biol Chem. 2012 Aug 6;287(41):34120–34133. doi: 10.1074/jbc.M112.359067

Table 1.

Peptide Sequence (H)1 (H)2 H)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.