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.