• Record: found
  • Abstract: found
  • Article: not found

Bacteria-selective synergism between the antimicrobial peptides alpha-helical magainin 2 and cyclic beta-sheet tachyplesin I: toward cocktail therapy.


Adult, Animals, Anti-Bacterial Agents, pharmacology, Antimicrobial Cationic Peptides, Binding Sites, Cell Membrane, physiology, Circular Dichroism, DNA-Binding Proteins, Drug Synergism, Erythrocytes, drug effects, Female, Fluoresceins, metabolism, Gram-Negative Bacteria, growth & development, Gram-Positive Bacteria, Hemolysis, Horseshoe Crabs, Humans, Magainins, Peptides, Cyclic, Phospholipids, Xenopus laevis, Protein Conformation, Skin, Xenopus Proteins

Read this article at

      There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.


      Magainin 2 and tachyplesin I (T-SS) are membrane-permeabilizing antimicrobial peptides discovered from frog skin and horseshoe crab hemolymph, respectively. They are classified into different secondary structural classes, i.e., alpha-helix and cyclic beta-sheet, respectively. We found that F5W-magainin 2 (MG2) and T-SS exhibited marked synergistic effects against Gram-negative and Gram-positive bacteria without enhancing hemolytic activity as a measure of toxicity. Dye release experiments using liposomes suggested that the selective synergism is mainly due to anionic phospholipid-specific synergism in membrane permeabilization. Furthermore, the cyclic structure of T-SS was found to be necessary for synergism because a linear analogue of T-SS did not show good synergism with MG2. These novel observations suggested the possibility of the development of cocktail therapeutic regimens using combinations of antimicrobial peptides.

      Related collections

      Author and article information



      Comment on this article