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. 2006 Feb;50(2):490–497. doi: 10.1128/AAC.50.2.490-497.2006

TABLE 1.

Peptides investigated and their properties

Peptide Designation Sequencea Acetonitrileb (%) Qc Mean MIC ± SDd (μM)
S4 ALWMTLLKKVLKAAAKAALNAVLVGANA 69 4 >32
K4K20S4ae P28 ---K---------------K--------NH2 60 7 8 ± 0
K4S4(1-16)a ---K------------NH2 49 6 4 ± 0
K4S4(1-15)a ---K-----------NH2 51 5 4 ± 0
K4S4(1-14)a P14 ---K----------NH2 50 5 4 ± 0
K4S4(1-13)a ---K---------NH2 47 5 32 ± 0
K4S4(1-12)a ---K--------NH2 47 5 32 ± 0
K4S4(1-10)a ---K------NH2 40 4 >32
Lauroyl-P14 C12-P14 CH3−(CH2)10−CONH−P14 74 4 >32
Aminolauroyl-P14 NC12-P14 NH2−(CH2)11−CONH−P14 55 5 2 ± 0
a

Primary structures of eight peptides in one-letter code (dashes represent residues identical to those in S4).

b

Hydrophobicity measure determined by reversed phase high-pressure liquid chromatography (percent acetonitrile/water eluent).

c

Electrical charge at physiological pH.

d

Minimal peptide concentration that caused 100% growth inhibition of 107 CFU of E. coli O157 after 24 h of incubation at 37°C in LB medium. Values represent the means and standard deviations obtained from three independent experiments performed in duplicates.

e

a, amide.