ArticleFrontiers in chemistry2020
Cyclic γ-Peptides With Transmembrane Water Channel Properties.
Article in Frontiers in chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 11 citations in OpenAlex.
- Chemically gated artificial nanochannels for programmable subcellular signal modulated transport regulation.Nature communications · 2025Article
- Inhibition of Ice Recrystallization by Nanotube-Forming Cyclic Peptides.Biomacromolecules · 2022Article
- Molecular Self-Assembly and Supramolecular Chemistry of Cyclic Peptides.Chemical reviews · 2021Review
- Transmembrane Self-Assembled Cyclic Peptide Nanotubes Based on α-Residues and Cyclic δ-Amino Acids: A Computational Study.Frontiers in chemistry · 2021Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Self-assembling peptides can be used to design new materials for medical and biological applications. Here we synthesized and characterized two novel cyclic γ-peptides (γ-CPs) with hydrophobic inner surfaces. The NMR and FT-IR studies confirmed that the CPs could self-assemble into parallel stacking structures via intermolecular H-bonds and π-π interactions. The morphologies of the self-assembly CPs showed bundles of nanotubes via transmission electron microscopy (TEM); these nanotubes form water channels to transport water across the lipid membrane. The properties of blocking the transport of protons like natural water channels showed that the hydrophobic inner surfaces are important in artificial transmembrane water channel designs. These studies also showed that water transport was a function of pore size and length of the assemblies.
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Registered trials
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