TABLE 2.

Sequences, α helicities, hydrophobicities, and hydrophobic moments of KSL and its analogs^a

Peptide	Sequence	% α helicity	H	M
KSL	K-K-V-V-F-K-V-K-F-K-NH2	56	−0.19	0.22
KSL1	K-K-V-V-V-K-V-K-F-K-NH2	42	−0.20	0.23
KSL2	K-K-V-V-F-K-F-K-F-K-NH2	43	−0.18	0.23
KSL3	K-K-L-L-F-K-L-K-F-K-NH2	70	−0.20	0.21
KSL4	K-K-V-L-F-K-L-K-F-K-NH2	42	−0.30	0.21
KSL5	K-K-V-V-P-K-V-K-F-K-NH2	—b	−0.30	0.30

^aα helicity was calculated from the mean residue ellipticity at 222 nm by the method of Chen et al. (14). Hydrophobicity (H) and hydrophobic moment (M) were calculated by the method of Eisenberg et al. (17). 

^bKSL5 had a random structure.