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Specific interactions of the antimicrobial peptide cyclic beta-sheet tachyplesin I with lipopolysaccharides
Yutaka Hirakura1, Satoe Kobayashi, Katsumi Matsuzaki
1Advanced Research Center for Human Sciences, Waseda University, Nishi-Tokyo, Tokyo 202-0021, Japan.
Biochimica Et Biophysica Acta
|May 4, 2002
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.