Table 1.

Sequences and calculated hydrophobicities of influenza HA host–guest fusion peptides of different lengths

^*The host segments of each peptide are underlined. 

^† The hydrophobic (negative on the respective scales of ref. 24) residues only are summed by using two different thermodynamic whole-residue hydrophobicity scales that should represent the transfer of unfolded peptides to the bilayer interface and into the hydrophobic interior of the lipid bilayer, respectively (24). Folding into an α-helix adds another −0.14 to −0.41 kcal/mol for each hydrogen-bonded residue in the interface (25, 26) and a likely more negative value in octanol.