Specific interactions of the antimicrobial peptide cyclic β-sheet tachyplesin I with lipopolysaccharides

The cyclic β-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 α-helical peptide F5W-magainin 2 (MG2) could not discriminate between LPS and acidic phospholipids. The recogn...

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Bibliographic Details
Published in:Biochimica et biophysica acta 2002-05, Vol.1562 (1), p.32-36
Main Authors: Hirakura, Yutaka, Kobayashi, Satoe, Matsuzaki, Katsumi
Format: Article
Language:English
Subjects:
1-Naphthylamine - analogs & derivatives
Amino Acid Sequence
Antimicrobial Cationic Peptides - chemistry
Antimicrobial peptide
Binding isotherm
Circular Dichroism
DNA-Binding Proteins - chemistry
Escherichia coli - chemistry
Fluorescent Dyes
Lipopolysaccharide
Lipopolysaccharides - chemistry
Liposomes - chemistry
Magainins
Molecular Sequence Data
Outer membrane permeabilization
Peptides, Cyclic - chemistry
Permeability
Protein Structure, Secondary
Tachyplesin I
Xenopus Proteins
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Summary:The cyclic β-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 α-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.
ISSN:0005-2736
0006-3002
1879-2642
DOI:10.1016/S0005-2736(02)00358-9