Antibiotic activity of reversed peptides of alpha-helical antimicrobial peptide, P18.
P18 (KWKLFKKIPKFLHLAKKF-NH(2)), an a-helical antimicrobial peptide designed from cecropin Amagainin 2 hybrid, was known to have potent antimicrobial activity against bacteria as well as fungi without hemolytic activity. To find the peptides comparable or superior to the antimicrobial activity of P18, the two reversed peptides (Rev-1 and Rev-2) of P18 were designed and synthesized. These peptides were found to have similar antimicrobial activity against bacterial and fungal cells without hemolytic activity as compared with P18. Furthermore, a reversed peptide, Rev-2 was shown to have a two-fold higher activity in killing some bacterial cells than P18. Therefore, these results suggested that Rev-2 peptide seems to be an excellent candidate for developing novel peptide antibiotics.
Lee
Si-Hyung
SH
Protein Engineering Laboratory, Korea Research Institute of Bioscience and Biotechnology, Yusong P.O. Box 115, Taejon, Korea.
Lee
Dong Gun
DG
Yang
Sung-Tae
ST
Kim
Yangmee
Y
Kim
Jae Il
JI
Hahm
Kyung-Soo
KS
Shin
Song Yub
SY
D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000494:pharmacology*; D001419:Bacteria / Q000187:drug effects; D005658:Fungi / Q000187:drug effects; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D013329:Structure-Activity Relationship
D023181:Antimicrobial Cationic Peptides; C447608:P18 antimicrobial peptide