Mohamed Amiche1, Aurelia Anne Seon1, Thierry Nicolas Pierre1, Pierre Nicolas1
1Laboratoire de Bioactivation des Peptides, Institut Jacques Monod, Université Paris 7, 2 Place Jussieu, 75251, Paris Cedex 05, France
Tóm tắt
Preprodermaseptins are a group of antimicrobial peptide precursors found in the skin of a variety of frog species. Precursors of this family have very similar N‐terminal preprosequences followed by markedly different C‐terminal domains that correspond to mature antimicrobial peptides. Some of these peptides are 24–34 amino acids long and form well‐behaved amphipathic α‐helices, others are disulfide‐linked peptides of 20–46 residues, still others, highly hydrophobic, are the smallest antimicrobial peptides known so far being only 10–13 residues in length. All these peptides are broad‐spectrum microbicides that kill many bacteria, protozoa, yeasts and fungi by destroying or permeating the microbial membrane. In frogs belonging to the genus Phyllomedusinae, preprodermaseptins encoded peptides also include dermorphins and deltorphins, D‐amino acid‐containing heptapeptides which are very potent and specific agonists of the μ‐ or δ‐opioid receptors. The remarkable similarity between preproregions of precursors that give rise to peptides with very different primary structures, conformations and activities suggests that the corresponding genes originate from a common ancestor. The high conservation of the precursor prepropart indicates that this region must have an important function.
