Table 2.

Biophysical data of the peptide analogs

Peptidesa	tR (min)b	Benignc		50% TFEd
	25°C	[θ]222	% helixe	[θ]222	% helixe
P	46.9	−14550	36.66	−39700	100.00
K7D	44.1	−6050	15.22	−30900	77.77
K14D	43.5	−15550	39.16	−35250	88.72
K22D	43.3	−8400	21.14	−33950	85.48
K7D/K14D	40.9	−8750	22.02	−28450	71.65
K14D/K22D	40.1	−6350	15.95	−32150	81.00
K7D/K14D/K22D	37.9	−5000	12.59	−26350	66.33
K7D/K10D/K14D/K22D	35.5	−7350	22.48	−19400	48.84
K3D/K7D/K10D/K14D/K22D	34.6	−4750	14.59	−21400	53.99
K1D/K3D/K7D/K10D/K14D/K22D	34.6	−5800	17.74	−19300	48.61
L6D	44.6	−8500	21.45	−39550	99.61
L12D	42.9	−8350	21.01	−37750	95.08
L20D	42.5	−6900	17.42	−36900	92.90
L6D/L12D	40.8	−6800	17.14	−29050	73.13
L12D/L20D	37.8	−5550	13.93	−30050	75.69
L6D/L12D/L20D	37.4	−4950	12.45	−28450	71.66
L6D/L12D /L17D/L20D	36.3	−4050	12.46	−15050	37.88
L6D/L12D /L17D/L20D /L21D	34.8	−3600	10.97	−13150	33.20

^aPeptides are ordered by relative hydrophobicity

^bt_R (min) denotes the retention time at 25°C by RP-HPLC

^cThe mean residue molar ellipticities, [θ]₂₂₂ (degree cm² dmol⁻¹) at wavelength 222 nm were measured at 25°C in KP buffer (100 mmol/L KCl, 50 mmol/L PO₄, pH 7.0)

^dThe mean residue molar ellipticities, [θ]₂₂₂ (degree cm² dmol⁻¹) at wavelength 222 nm were measured at 25°C in KP buffer with 50% TFE

^eThe helical content (in percentage) of a peptide relative to the molar ellipticity value of peptide P in 50% TFE