Abstract.
Plasticins belong to the dermaseptin superfamily of gene-encoded, membrane-active host defense peptides produced by the skin of hylid frogs. The plasticins, which are rich in Gly and Leu residues arranged in regular 5-mer motifs GXXXG (where X is any amino acid residue), have very similar amino acid sequences, hydrophobicities, and amphipathicities but differ markedly in their net charge, conformational plasticity, and activity spectra. The intrinsic flexibility and structural malleability of plasticins modulate their ability to bind to and disrupt the membranes of prokaryotic and eukaryotic cells, and/or to reach intracellular targets, therefore triggering functional versatility. This family of closely related but functionally divergent peptides constitutes a good model to address the relationships between structural polymorphism, membrane-interacting properties, and the biological activity of antimicrobial, cell-penetrating, and viral fusion peptides. Plasticins could thus serve as templates to design potent multifunctional drugs that could act simultaneously against bacterial pathogens and viruses.
Similar content being viewed by others
Author information
Authors and Affiliations
Corresponding author
Additional information
Received 26 September 2007; received after revision 22 October 2007; accepted 29 October 2007
Rights and permissions
About this article
Cite this article
El Amri, C., Nicolas, P. Plasticins: membrane-damaging peptides with ‘chameleon-like’ properties. Cell. Mol. Life Sci. 65, 895–909 (2008). https://doi.org/10.1007/s00018-007-7445-8
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00018-007-7445-8