Ionic pores formed by cyclic peptides.
It is shown that 2 cyclic tetrapeptides, namely tentoxin and HC toxin, are able to induce the formation of transmembrane ionic channels, although a carrier mechanism could be expected on the basis of their chemical structure (presence of proline or N-methylated residues). Since other cyclic peptides but of larger size, i.e., tyrocidines, gramicidin S (decapeptides) and an octapeptide with a sequence similar to that of HC toxin, are also able to form pores, it appears that this property can be extended to a large number of cyclic peptides. A pore structure based on aggregates is proposed.
Heitz
F
F
Laboratoire de Physico-Chimie des Systèmes Polyphasés, UA-330 du CNRS, Montpellier, France.
Kaddari
F
F
Van Mau
N
N
Verducci
J
J
Raniri Seheno
H
H
Lazaro
R
R
D002942:Circular Dichroism; D004594:Electrophysiology; D007473:Ion Channels / Q000187:drug effects*; D008051:Lipid Bilayers; D008956:Models, Chemical; D010456:Peptides, Cyclic / Q000494:pharmacology*
D007473:Ion Channels; D008051:Lipid Bilayers; D010456:Peptides, Cyclic; C037654:HC toxin; C003384:tentoxin