Conformations, cation binding, and transmembrane ion transfer properties of a cyclooctapeptide built by an alternation of D and L residues.
The conformations of a cyclic octapeptide built with an alternation of D and L residues are investigated on the basis of 1H n.m.r. and CD data. The cyclooctapeptide can form structures which are specific to the alternating D-L sequence. This peptide can form two types of complexes with cations (peptide 2-cation and peptide-cation complexes) and the binding with monovalent cation is weak. This peptide is able to induce transmembrane ion transfer through both a carrier mechanism and pore formation.
Heitz
F
F
Laboratory of Polyphasic System Physiochemistry, UA 330, Montpellier, France.
Kaddari
F
F
Heitz
A
A
Raniriseheno
H
H
Lazaro
R
R
D000097:Acetonitriles; D000595:Amino Acid Sequence; D002412:Cations; D002725:Chloroform; D002942:Circular Dichroism; D004121:Dimethyl Sulfoxide; D007473:Ion Channels / Q000378:metabolism*; D008094:Lithium / Q000378:metabolism; D008274:Magnesium / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010456:Peptides, Cyclic / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D013237:Stereoisomerism
D000097:Acetonitriles; D002412:Cations; D007473:Ion Channels; D010456:Peptides, Cyclic; C062624:cyclo(alanyl-alanyl-2-amino-9-decanoic acid-prolyl)(2); D002725:Chloroform; D008094:Lithium; D008274:Magnesium; D004121:Dimethyl Sulfoxide; C032159:acetonitrile