TABLE 1.
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 |
Primary structures of eight peptides in one-letter code (dashes represent residues identical to those in S4).
Hydrophobicity measure determined by reversed phase high-pressure liquid chromatography (percent acetonitrile/water eluent).
Electrical charge at physiological pH.
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.
a, amide.