Literature DB >> 11988219

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

Yutaka Hirakura1, Satoe Kobayashi, Katsumi Matsuzaki.   

Abstract

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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Year:  2002        PMID： 11988219     DOI： 10.1016/s0005-2736(02)00358-9

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  13 in total

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