Design, synthesis, and characterization of peptide nanostructures having ion channel activity

Biron, Éric; Otis, François; Meillon, Jean‐Christophe; Robitaille, Martin; Lamothe, Julie; Hove, Patrick Van; Cormier, Marie-Eve; Voyer, Normand

doi:10.1016/j.bmc.2003.08.037

Cited by 69 publications

(64 citation statements)

References 63 publications

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“…The first such example was reported by Fernandez-Lopez and Ghadiri and their co-workers [30]. Voyer and co-workers [46], as noted above, developed a family of compounds in which crown ethers were appended to α-helical peptide chains. These 'crown peptides' did not exhibit activity against Gram-positive bacteria, but proved to be cytotoxic to breast cancer (MDA) cells and to mouse leukemia (P388) cells.…”

Section: Biological Activity Of Synthetic Cation Channelsmentioning

confidence: 98%

Synthetic, Biologically Active Amphiphilic Peptides

Yamnitz

Gokel

2007

Chemistry & Biodiversity

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Amphiphilic peptides typically consist of a peptide portion that may be 5-25 (or more) amino acids in length. The hydrophobic portion may be a single fatty acid residue, but can also be more elaborate. The main focus of this article lies on the family of synthetic anion binders (SATs) of the general structure (R 1 ) 2 N-COCH 2 OCH 2 CO-(Aaa) n -OR 3 . The most-common R 1 groups are octadecyl (C 18 H 37 ). The most studied peptide sequence in this family is (Gly) 3 -Pro-(Gly) 3 , although different sequences (and longer and shorter peptides) have been prepared as well. The C-terminal ester residue providing the most effective anion release from liposomes is heptyl (C 7 H 15 ), although many others have been examined. The compound (C 18 H 37 ) 2 N-COCH 2 OCH 2 CO-(Gly) 3 -Pro-(Gly) 3 -OBn (Bn=benzyl) was found to mediate Cl -transport in mouse epithelial cells.

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Section: Biological Activity Of Synthetic Cation Channelsmentioning

confidence: 98%

Synthetic, Biologically Active Amphiphilic Peptides

Yamnitz

Gokel

2007

Chemistry & Biodiversity

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“…(ii) The NH 3 -NH 6 proton chemical shifts are remarkably insensitive to the DMSO addition. (iii) The sensitivity of the NH 2 proton chemical shift is intermediate.…”

Section: Conformational Analysismentioning

confidence: 99%

“…They can be easily assembled in structurally well-defined, nanometer-scale, architectures of bis-crown as well as polymeric crown compounds on a peptide framework. [4][5][6] In the past few years, a series of crown-carrier derivatives of -DOPA, [4][5][6][7][8][9][10][11][12][13][14][15][16] -Lys, [17] or -Glu, [18] have been synthesized for the construction of specific peptide receptors for alkali metal, ammonium and di-ammonium ions. Application of this concept to C α -tetrasubstituted α-amino acids should result in more defined and predictable peptide structures, as ability was carried out.…”

Section: Introductionmentioning

confidence: 99%

Synthesis, Ion Complexation Study, and 3D‐Structural Analysis of Peptides Based on Crown‐Carrier, C^α‐Methyl‐L‐DOPA Amino Acids

Wright¹,

Anddad²,

Lohier³

et al. 2008

Eur J Org Chem

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Selected series of terminally protected model peptides to the hexamer level, based on four novel, crown‐ether containing Cα‐methyl‐L‐DOPA (L‐Mdp) amino acid residues, namely L‐Mdp[15‐C‐5], L‐Mdp[18‐C‐6], L‐Mdp[benzo‐24‐C‐8] and L‐Mdp[(S)‐Binol‐20‐C‐6], combined with either L‐Ala or L‐Ala/Aib or Gly/Aib, were synthesized by solution methods. An ESI‐MS analysis of their alkali metal cation complexation ability was carried out. Their FTIR absorption, 1H NMR, ECD, and VCD spectroscopic properties suggest that all of these crowned amino acids are strong inducers of (left‐handed) β‐turns and 310‐helical structures.(© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2008)

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“…Previous studies showed that they exist mainly in a helical conformation, in which the crown ether side chains can align as a stack (Figures B and C) to form monomeric functional ion channels . Such nanostructures have been shown to be efficient toxins against breast cancer and leukemia cancer cells …”

Section: Introductionmentioning

confidence: 96%

Crown ether helical peptides are preferentially inserted in lipid bilayers as a transmembrane ion channels

et al. 2015

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Oriented circular dichroism was used to study the alignment crown ether-modified peptides. The influence of different N-and C-functionalities was assessed using at variable peptide:lipid ratios from 1:20 to 1:200. Neither the functionalities nor the concentration had any major effect on the orientation. The alignment of the 21-mer peptides was also examined with lipid membranes of different bilayer thickness. The use of synchrotron radiation as light source allowed the study of peptide:lipid molar ratios from 1:20 to 1:1000. For all conditions studied, the peptides were found to be predominantly incorporated as a transmembrane helix into the membrane, especially at low peptide concentration, but started to aggregate on the membrane surface at higher peptide:lipid ratios. The structural information on the preferred trans-bilayer alignment of the crown ether functional groups explains their ion conductivity and is useful for the further development of membrane-active nanochemotherapeutics.

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Design, synthesis, and characterization of peptide nanostructures having ion channel activity

Cited by 69 publications

References 63 publications

Synthetic, Biologically Active Amphiphilic Peptides

Synthetic, Biologically Active Amphiphilic Peptides

Synthesis, Ion Complexation Study, and 3D‐Structural Analysis of Peptides Based on Crown‐Carrier, C^α‐Methyl‐L‐DOPA Amino Acids

Crown ether helical peptides are preferentially inserted in lipid bilayers as a transmembrane ion channels

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Design, synthesis, and characterization of peptide nanostructures having ion channel activity

Cited by 69 publications

References 63 publications

Synthetic, Biologically Active Amphiphilic Peptides

Synthetic, Biologically Active Amphiphilic Peptides

Synthesis, Ion Complexation Study, and 3D‐Structural Analysis of Peptides Based on Crown‐Carrier, Cα‐Methyl‐L‐DOPA Amino Acids

Crown ether helical peptides are preferentially inserted in lipid bilayers as a transmembrane ion channels

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Synthesis, Ion Complexation Study, and 3D‐Structural Analysis of Peptides Based on Crown‐Carrier, C^α‐Methyl‐L‐DOPA Amino Acids