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XB-ART-7197
Biochim Biophys Acta 2002 May 03;15621-2:32-6. doi: 10.1016/s0005-2736(02)00358-9.
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Specific interactions of the antimicrobial peptide cyclic beta-sheet tachyplesin I with lipopolysaccharides.

Hirakura Y , Kobayashi S , Matsuzaki K .


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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.

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Species referenced: Xenopus
Genes referenced: magainins