TABLE 1.
Peptide | Sequencea |
---|---|
LL-37 | NH2-LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES-COOH |
EFK17 | NH2-E1FKR2IVQR2IKD3FLRN3L4V-COOH |
d | NH2-EdFKRdIVQRdIKDdFLRNLV-COOH |
W | NH2-EWKRWVQRWKDWLRNLV-COOH |
a | CH3CONH-EFKRIVQRIKDFLRNLV-CONH2 |
d/a | CH3CONH-EdFKRdIVQRdIKDdFLRNLV-CONH2 |
W/a | CH3CONH-EWKRWVQRWKDWLRNLV-CONH2 |
In the LL-37 sequence, the internal EFK17 segment is highlighted in boldface type, as are the modification sites on the EFK17 variants. All EFK17 variants have a net charge of +3 at pH 7.4 and a pI of ∼11. The known proteolytic cleavage sites within EFK17 are marked for V8 protease, aureolysin, and Pseudomonas aeruginosa elastase (PE) and are shown as 1 to 4 (43, 47). 1, V8 and PE; 2, aureolysin and PE; 3, PE; 4, aureolysin.