Table 2.

Biophysical data of the peptide analogs.

Peptide a	tR(min) b	Benign c		50%TFE d
		[θ]222	% helix e	[θ]222	% helix e
V16K	32.2	−1,990	6.6	−29,313	97.5
V16G	33.6	−2,839	9.4	−27,857	92.7
V16S	34.3	−1,760	5.9	−28,949	96.3
V16E	34.6	−3,465	11.5	−30,063	100.0
V16A	36.6	−3,057	10.2	−28,769	95.7
P	38.2	−2,592	8.6	−29,726	98.9
V16L	40.4	−3,595	12.0	−29,803	99.1

^a Peptides are ordered by relative hydrophobicity during RP-HPLC at 25 °C. ^b Retention times of peptides during RP-HPLC at 25 °C. ^c The mean residue molar ellipticities, [θ]₂₂₂(degree·cm²· dmol⁻¹) at wavelength 222 nm were measured at 25 °C in KP bsuffer (100 mM KCl, 50 mM K₂HPO₄/KH₂PO₄, pH 7.0). ^d The mean residue molar ellipticities, [θ]₂₂₂(degree·cm²·dmol⁻¹) at wavelength 222 nm were measured at 25 °C in KP buffer diluted 1:1 (v/v) with TFE. ^e The helical content (in percentage) of a peptide relative to the molar ellipticity value of peptide V16E in 50% TFE.