Formation of ion-selective channel using cyclic tetrapeptides

Suga, Torao; Osada, Shinji; Kodama, Hiroaki

doi:10.1016/j.bmc.2011.11.036

Cited by 14 publications

(11 citation statements)

References 18 publications

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“…Cyclic peptides that contain alternating α-D,L amino acids have therefore been an attractive template to form well-defined nanotubes and channels with cavity diameters ranging from 2 to 13 Å. 13,[28][29][30][31][32] Another appealing feature of these self-assembling cyclic peptides is that the alternating absolute configuration projects the amino acid side chains out of the plane of the cyclic peptide and enables chemical modification of the peptide side chains without causing significant interference with the extensive hydrogen bonding perpendicular to the plane of the cyclic peptide.…”

Section: Introductionmentioning

confidence: 99%

“…Functionalization of the cyclic peptide side chains with (macro)molecules and the effect upon the properties of nanotubes [33][34][35][36][37][38] and artificial channels [39][40][41] is an exciting recent development of these systems. Although, the effect of the amino acid configuration and type of peptide side chains upon artificial channel formation has been studied, 13,[27][28][29][30]39,[42][43][44] only a selection of studies have investigated the lipid bilayer partitioning of self-assembling cyclic peptides that contain non-natural βor γ-amino acids. 45,46 To the best of our knowledge, no previous study conducted has described the effects on lipid bilayer partitioning of octameric cyclic peptides that contain non-natural α-L-amino acids.…”

Section: Introductionmentioning

confidence: 99%

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Effect of the amino acid composition of cyclic peptides on their self-assembly in lipid bilayers

2015

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The effect of amino acid composition on the formation of transmembrane channels in lipid bilayers upon self-assembly of alt-(L,D)-α-cyclic octapeptides has been investigated. Cyclic peptides comprising D-leucine, alternating with different combinations of L-azidolysine, L-lysine(Alloc), L-lysine and L-tryptophan were synthesized and the size of pores formed via self-assembly of these molecules in lipid bilayers was elucidated using large unilamellar vesicle fluorescence assays and dynamic light scattering. Pore formation was examined in large unilamellar vesicles made up of egg yolk phosphatidylcholine or Escherichia coli total lipid extract. From these analyses, we have established that cyclic peptides with charged side chains form large pores while those with neutral side chains form unimeric pores. Furthermore, the cyclic peptides that consist of non-symmetric amino acid configurations possess a higher membrane activity than the cyclic peptides with a symmetric amino acid configuration. In addition, we have found that peptide amphiphilicity plays a vital role in selective partitioning between bilayers that consist of egg yolk phosphatidylcholine and those comprised of E. coli total lipid extract. These results suggest that selective transbilayer channel formation via self-assembly may be a viable alternative for many applications that currently use more expensive, multistep synthesis methods.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Effect of the amino acid composition of cyclic peptides on their self-assembly in lipid bilayers

2015

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“…This strong hydrogen bonding facilitates purification of CP NTs through precipitation of aggregates, thus obviating the need for chromatographic purification. Further, the planar structure of the CP backbone projects the peptide side chains from the external periphery leaving a hollow channel with a van der Waals diameter ranging from 0.2 to 1.3 nm, for CPs incorporating 4-12 amino-acid residues, respectively 14,15,[17][18][19] . Although a range of CPs with different ring sizes can be synthesized, model studies using N-alkylated CP dimers indicate that CPs with eight amino-acid residues have the highest association constants 15,20 .…”

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confidence: 99%

Janus cyclic peptide–polymer nanotubes

et al. 2013

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Self-assembled nanotubular structures have numerous potential applications but these are limited by a lack of control over size and functionality. Controlling these features at the molecular level may allow realization of the potential of such structures. Here we report a new generation of self-assembled cyclic peptide-polymer nanotubes with dual functionality in the form of either a Janus or mixed polymeric corona. A 'relay' synthetic strategy is used to prepare nanotubes with a demixing or mixing polymeric corona. Nanotube structure is assessed in solution using 1 H-1 H nuclear Overhauser effect spectroscopy NMR, and in bulk using differential scanning calorimetry. The Janus nanotubes form artificial pores in model phospholipid bilayers. These molecules provide a viable pathway for the development of intriguing nanotubular structures with dual functionality via a demixing or a mixing polymeric corona and may provide new avenues for the creation of synthetic transmembrane protein channel mimics.

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“…who observed electron (and optical) microscopy images of unconjugated CPs in bundles (microcrystals) . We interpret the SANS patterns to mean that CP1 exists as bundles of short tubes in [D 6 ]DMSO, a concept that has also been proposed in the study of CP ion channel mechanism . Indeed, although early work in the field presented the mechanism of ion transport through the internal cavities of cyclic peptide nanotubes, assembly into ‘barrel and stave’ structures has also been suggested .…”

Section: Resultsmentioning

confidence: 74%

“…and Kodama et al. have shown that the transport of ions is possible with cyclic peptides with only 4 or 6 residues, for which the internal pore is too small to allow ion transport, thus suggesting a barrel and stave assembly …”

Section: Resultsmentioning

confidence: 99%

Study of (Cyclic Peptide)–Polymer Conjugate Assemblies by Small‐Angle Neutron Scattering

Koh

FitzGerald

Warr

et al. 2016

Chemistry A European J

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Copyright and reuse:The Warwick Research Archive Portal (WRAP) makes this work by researchers of the University of Warwick available open access under the following conditions. Copyright © and all moral rights to the version of the paper presented here belong to the individual author(s) and/or other copyright owners. To the extent reasonable and practicable the material made available in WRAP has been checked for eligibility before being made available.Copies of full items can be used for personal research or study, educational, or not-for profit purposes without prior permission or charge. Provided that the authors, title and full bibliographic details are credited, a hyperlink and/or URL is given for the original metadata page and the content is not changed in any way. A note on versions:The version presented here may differ from the published version or, version of record, if you wish to cite this item you are advised to consult the publisher's version. Please see the 'permanent WRAP url' above for details on accessing the published version and note that access may require a subscription. AbstractWe present a fundamental study into the self-assembly of (cyclic peptide)-polymer conjugates as a versatile supramolecular motif to engineer nanotubes with defined structure and dimensions, as characterised in solution using small angle neutron scattering (SANS).This work demonstrates the ability of the grafted polymer to stabilise and/or promote the formation of unaggregated nanotubes by the direct comparison to the unconjugated cyclic peptide precursor. This ideal case permitted a further study into the growth mechanism of self-assembling cyclic peptides, allowing an estimation of the cooperativity. Furthermore we show the dependency of the nanostructure on the polymer and peptide chemical functionality in solvent mixtures that vary in the ability to compete with the intermolecular associations between cyclic peptides and ability to solvate the polymer shell.

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Formation of ion-selective channel using cyclic tetrapeptides

Cited by 14 publications

References 18 publications

Effect of the amino acid composition of cyclic peptides on their self-assembly in lipid bilayers

Effect of the amino acid composition of cyclic peptides on their self-assembly in lipid bilayers

Janus cyclic peptide–polymer nanotubes

Study of (Cyclic Peptide)–Polymer Conjugate Assemblies by Small‐Angle Neutron Scattering

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