TABLE 2.

Ellipticity, tryptophan fluorescence emission shift, and activities of MesY105 and its derivatives^a

Peptide	% by CDb				Fluorescence emission shift (Δλmaxc [nm])	Biological activity (MICd [nM])
	Aqueous buffer		C13-LPC micelles (Ri = 40)
	Unstructured	Hα	Unstructured	Hα
MesY105	68	7	26	24	9	1.6
H8Y	50	10	59	17	11	31
H8L	64	9	31	22	10	83
G13E	45	13	46	19	6	130
S15F	58	8	37	23	10	4.1
W18F	76	5	27	24	9	21
A21V	61	6	37	24	13	73
A24P	58	9	60	15	4	9,700
R28H	66	8	73	9	1	20,000
W37F	77	4	37	21	14	47
Mes36	76	6	52	14	6	27,000

^aStandard deviations are less than 5%.

^bPercentage of amino acid residues in unstructured or α-helix state.

^cChange in the maximum fluorescence emission wavelength observed upon addition of LPC micelles.

^dMIC data were obtained with at least three independent activity assays against L. ivanovii Li4(pVS2) (2).