Conformations, cation binding, and transmembrane ion transfer properties of a cyclooctapeptide built by an alternation of D and L residues.

International Journal of Peptide and Protein Research
F HeitzR Lazaro

Abstract

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.

References

Jan 1, 1989·Biochimie·F HeitzR Lazaro
Dec 1, 1987·International Journal of Peptide and Protein Research·F HeitzR Lazaro
Jul 1, 1987·International Journal of Peptide and Protein Research·R JacquierP Viallefont
Mar 1, 1986·Biophysical Chemistry·F HeitzJ Verducci
Dec 17, 1974·Biochemistry·W R VeatchE R Blout
Jun 1, 1972·Proceedings of the National Academy of Sciences of the United States of America·D W Urry

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Citations

Feb 23, 2019·Proceedings of the National Academy of Sciences of the United States of America·Suzanne M BatisteBjorn C Knollmann
Dec 21, 2002·The Journal of Peptide Research : Official Journal of the American Peptide Society·J RameshK R K Easwaran
Dec 16, 2016·Proceedings of the National Academy of Sciences of the United States of America·Suzanne M Batiste, Jeffrey N Johnston
Mar 23, 2018·Journal of the American Chemical Society·Suzanne M Batiste, Jeffrey N Johnston

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