Anion transport in liposomes responds to variations in the anchor chains and the fourth amino acid of heptapeptide ion channels

Riccardo Ferdani, Robert Pajewski, Natasha Djedovič, Jolanta Pajewska, Paul H. Schlesinger, George W. Gokel

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

Seven heptapeptide derivatives have been prepared. The peptide structure is (Gly)3Xxx(Gly)3 in which Xxx stands for a variable amino acid. The amino acid variations include azetidine carboxylic acid, pipecolic acid, meta-aminobenzoic acid, proline, and leucine. All seven compounds have a C-terminal benzyl group. In all cases, the heptapeptide's N-terminus was linked to diglycolic acid and a dialkylamine. In five cases, the N-terminal group was didecylamine and in two cases, N-ethyl-N-decyl. Chloride and carboxyfluorescein release from phospholipid vesicles was studied with the result that C 10H21N(C2H5)COCH2OCH 2CO-NH-(Gly)3Leu(Gly)3-OCH2Ph was the most active. Hill analysis showed that this compound involves pore formation by four monomer units rather than two, as previously found for other members of this family.

Original languageEnglish
Pages (from-to)673-680
Number of pages8
JournalNew Journal of Chemistry
Volume29
Issue number5
DOIs
StatePublished - May 2005

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