Table 1. Peptide designation and properties.
Peptide designation | Sequencea | Net charge | Molecular mass (g/mole) | Charge densityb | Hydrophobicity (% AcN)c |
K9L6 | LKKLKKLLKKLKKKL-NH2 | +10 | 1849.7 | 0.667 | 36.7 |
5D-K6L9 | LKLLKKLLKKLLKLL-NH2 | +7 | 1805.4 | 0.467 | 55.6 |
K6L9 | KLLKKLLKKLLKLL-NH2 | +7 | 1805.4 | 0.467 | 67.2 |
K5L7 | KKLLKLLLKLLK-NH2 | +6 | 1451.0 | 0.500 | 56.5 |
C8-K5L7 | CH3(CH2)6CO-KKLLKLLLKLLK-NH2 | +5 | 1564.0 | 0.416 | 61.4 |
LL-37 | LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES-NH2 | +7 | 4493.3 | 0.324 | 67.6 |
Magainin 2 | GIGKFLHSAKKFGKAFVGEIMNS-NH2 | +4 | 2466.9 | 0.227 | 67.1 |
Polymyxin B | C50H100N16O17S | +5 | 1301.5 | 0.455 | 53.2 |
Colistin | C52H98N16O13 | +5 | 1155.5 | 0.455 | ND |
Underlined and bold amino acids are D-enantiomers. All linear peptides are amidated in their C-terminus.
Calculated by dividing the net charge by the total number of amino acids.
The peptides were eluted in 40 min using a linear gradient of acetonitrile (AcN) from 30 to 70% v/v in water containing TFA (0.05% v/v) on a C4 reverse analytical column.