Specific interactions of the antimicrobial peptide cyclic beta-sheet tachyplesin I with lipopolysaccharides.
The cyclic beta-sheet antimicrobial peptide tachyplesin I (T-SS) was found to show 280-fold higher affinity for lipopolysaccharides (LPS) compared with acidic phospholipids, whereas the linear alpha-helical peptide F5W-magainin 2 (MG2) could not discriminate between LPS and acidic phospholipids. The recognition site was the lipid A moiety and the cyclic structure was crucial to this specific binding. The cyclic structure also endowed the peptide with very rapid outer membrane (OM) permeabilization.
Hirakura
Yutaka
Y
Advanced Research Center for Human Sciences, Waseda University, Nishi-Tokyo, Tokyo 202-0021, Japan.
Kobayashi
Satoe
S
Matsuzaki
Katsumi
K
D015057:1-Naphthylamine / Q000031:analogs & derivatives*; D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry*; D002942:Circular Dichroism; D004268:DNA-Binding Proteins / Q000737:chemistry*; D004926:Escherichia coli / Q000737:chemistry; D005456:Fluorescent Dyes; D008070:Lipopolysaccharides / Q000737:chemistry*; D008081:Liposomes / Q000737:chemistry; D054806:Magainins; D008969:Molecular Sequence Data; D010456:Peptides, Cyclic / Q000737:chemistry*; D010539:Permeability; D017433:Protein Structure, Secondary; D029867:Xenopus Proteins
D023181:Antimicrobial Cationic Peptides; D004268:DNA-Binding Proteins; D005456:Fluorescent Dyes; D008070:Lipopolysaccharides; D008081:Liposomes; D054806:Magainins; D010456:Peptides, Cyclic; D029867:Xenopus Proteins; C053301:magainin 2 peptide, Xenopus; C057636:tachyplesin peptide, Tachypleus tridentatus; C005444:N-phenyl-1-naphthylamine; D015057:1-Naphthylamine