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. Author manuscript; available in PMC: 2012 Sep 20.
Published in final edited form as: Biochemistry. 2011 Aug 26;50(37):7919–7932. doi: 10.1021/bi200873u

Table 1.

Parent Set of Peptides and Sets 1 and 2 of Mutants. (Unless indicated, N- and C-termini are free.)

Peptide Charge (pH 7.5) Length (residues) μHa Sequence
Set of Parent Peptides
δ-Lysin 0 26 7.8 formyl-MAQDIISTIGDLVKWIIDTVNKFTKK
Cecropin A +7 37 4.9 KWKLFKKIEKVGQNIRDGIIKAGPAVAVVGQATQIAK-amide
Magainin-2 F12W +3 23 6.9 GIGKFLHSAKKWGKAFVGEIMNS

Set 1 of Mutant Peptides
DL-1 +6 26 7.2 formyl-MAQKIISTIGKLVKWIIKTVNKFTKK
CE-1 +1 37 7.3 EWKLFEKIEKLGQNILDGIIKLGPLLALLGQLTQIAL-amide
MG-1 0 23 9.1 GILKFLESAKKWLEAFLAEIMNS

Set 2 of Mutant Peptides
DL-2a 0 26 7.7 formyl-LAADLLAALGDLAKWLLDALAKAAKK
DL-2b 0 26 8.8 formyl-LAADLLAALGDLLKWLLDALAKLAKK
CE-2 +7 37 5.2 KWKLLKKLEKAGAALKEGLLKAGPALALLGAAAALAK-amide
MG-2 +3 23 7.0 GLGKLLHAAKKLGKAWLGELLAA
a

Hydrophobic moment of the complete helix calculated with MPEx using the Wimley-White interfacial scale (18).