Intrinsic flexibility and structural adaptability of Plasticins membrane-damaging peptides as a strategy for functional versatility.
The Plasticins are a family of antimicrobial, 23-29-residue Gly-Leu-rich ortholog peptides from the frog skin that have very similar amino acid sequences, hydrophobicities, and amphipathicities but differ markedly in their conformational plasticity and spectrum of activity. The intrinsic flexibility and structural malleability of Plasticins modulate their ability to bind to and disrupt the bilayer membranes of prokaryotic and eukaryotic cells, and/or to reach intracellular targets, therefore, triggering functional versatility. The discussion is opened herein on several examples of other membrane-active peptides, like viral fusion peptides, cell-penetrating peptides, that are able to display antimicrobial activity. Hence, Plasticins could be regarded as models of multipotent membrane-active peptides guided by structural plasticity.
El Amri
C
C
FRE 2852 Protéines: Biochimie Structurale et Fonctionnelle, Université Paris 6-CNRS, Peptidome de la peau d'amphibiens, tour 43, 4, Place Jussieu 75252, Paris Cedex 05, France. elamri@ccr.jussieu.fr
Bruston
F
F
Joanne
P
P
Lacombe
C
C
Nicolas
P
P
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D001001:Anura; D005136:Eye Proteins / Q000737:chemistry*; D006801:Humans; D008566:Membranes / Q000737:chemistry / Q000187:drug effects*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry*; D011487:Protein Conformation
D000900:Anti-Bacterial Agents; D005136:Eye Proteins; D009419:Nerve Tissue Proteins; C076104:plasticin