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

doi:10.1039/b417808b

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 journal › Article › peer-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 language	English
Pages (from-to)	673-680
Number of pages	8
Journal	New Journal of Chemistry
Volume	29
Issue number	5
DOIs	https://doi.org/10.1039/b417808b
State	Published - May 2005

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

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.",

author = "Riccardo Ferdani and Robert Pajewski and Natasha Djedovi{\v c} and Jolanta Pajewska and Schlesinger, {Paul H.} and Gokel, {George W.}",

year = "2005",

month = may,

doi = "10.1039/b417808b",

language = "English",

volume = "29",

pages = "673--680",

journal = "New Journal of Chemistry",

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TY - JOUR

T1 - Anion transport in liposomes responds to variations in the anchor chains and the fourth amino acid of heptapeptide ion channels

AU - Ferdani, Riccardo

AU - Pajewski, Robert

AU - Djedovič, Natasha

AU - Pajewska, Jolanta

AU - Schlesinger, Paul H.

AU - Gokel, George W.

PY - 2005/5

Y1 - 2005/5

N2 - 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.

AB - 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.

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U2 - 10.1039/b417808b

DO - 10.1039/b417808b

M3 - Article

C2 - 19169373

AN - SCOPUS:19544381884

SN - 1144-0546

VL - 29

SP - 673

EP - 680

JO - New Journal of Chemistry

JF - New Journal of Chemistry

IS - 5

ER -

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

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