Cyclic γ-Peptides With Transmembrane Water Channel Properties

Chen, Jie; Li, Qiang; Wu, Pengchao; Liu, Juan; Wang, Dan; Yuan, Xiaohong; Zheng, Renlin; Sun, Rongqin; Li, Liangchun

doi:10.3389/fchem.2020.00368

Cited by 7 publications

(3 citation statements)

References 38 publications

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“…Having established that the aggregates are β-sheet rich, we performed Fourier-transform infrared (FTIR) experiments to shed further light on their secondary structure. In line with the CD results, Lys2CP8 in solid-state displayed a number of bands at frequencies characteristic for β-sheet structures , (Figure a), such as the CO amide-I band at 1630 cm –1 . This is typically attributed to the formation of antiparallel β-sheets between peptide backbones.…”

Section: Results and Discussionmentioning

confidence: 99%

Inhibition of Ice Recrystallization by Nanotube-Forming Cyclic Peptides

et al. 2022

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While most native ice-binding proteins are rigid, artificial (macro)molecular ice-binders are usually flexible. Realizing a regular array with precisely positioned ice-binding motifs on synthetic proteins, (macro)molecular ice-binders are thus challenging. Here, we exploit the predictable assembly of cyclic peptides into nanotubes as a starting point to prepare large, rigid ice-binders bearing an ice-binding site that is found in hyperactive ice-binding proteins in insects. First, we designed, synthesized, and purified cyclic octapeptide Lys2CP8 bearing a TaT motif to promote ice binding and investigated their solution assembly and activity using circular dichroism (CD) spectroscopy, Fourier-transform infrared (FTIR) spectroscopy, light scattering (LS), cryogenic transmission electron microscopy (cryo-TEM), and ice recrystallization inhibition (IRI) assays. The cyclic peptide Lys2CP8 was synthesized in good yield using Fmoc chemistry and purified by reversed-phase HPLC. Upon dissolution in aqueous solutions, Lys2CP8 was observed to assemble in a pH- and concentration-dependent manner into objects with nanoscopic dimensions. LS revealed the presence of small and large aggregates at pH 3 and 11, held together through a network of intermolecular antiparallel β-sheets as determined by FTIR and CD spectroscopy. Cryo-TEM revealed the presence of one-dimensional objects at pH 3 and 11. These are mostly well-dispersed at pH 3 but appear to bundle at pH 11. Interestingly, the pH-dependent self-assembly behavior translates into a marked pH dependence of IRI activity. Lys2CP8 is IRI-active at pH 3 while inactive at pH 11 hypothetically because the ice-binding sites are inaccessible at pH 11 due to bundling.

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Section: Results and Discussionmentioning

confidence: 99%

Inhibition of Ice Recrystallization by Nanotube-Forming Cyclic Peptides

et al. 2022

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“…The cyclic peptide 44 readily assembles into nanotubes in acetonitrile with a methyl group pointing toward the interior. Finally, cyclic peptides composed of only γ-amino acids could be designed by replacing any α-amino acid residue with its chiral counterpart of γ-Aca (Figure b). − The self-assembling behavior of the γ-cyclic peptides were shown to vary depending on the ring size. Tetrapeptides ( 45 ) or hexapeptides ( 46 ) self-assemble into nanotubes through parallel-type hydrogen bonding interactions, while octapeptides ( 47 ) interact with each other via antiparallel β-sheet-type hydrogen bonding.…”

Section: Tubular Ensembles Of Cyclic Peptidesmentioning

confidence: 99%

Molecular Self-Assembly and Supramolecular Chemistry of Cyclic Peptides

et al. 2021

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This Review focuses on the establishment and development of self-assemblies governed by the supramolecular interactions between cyclic peptides. The Review first describes the type of cyclic peptides able to assemble into tubular structures to form supramolecular cyclic peptide nanotubes. A range of cyclic peptides have been identified to have such properties, including α-peptides, β-peptides, α,γ-peptides, and peptides based on δ- and ε-amino acids. The Review covers the design and functionalization of these cyclic peptides and expands to a recent advance in the design and application of these materials through their conjugation to polymer chains to generate cyclic peptide–polymer conjugates nanostructures. The Review, then, concentrates on the challenges in characterizing these systems and presents an overview of the various analytical and characterization techniques used to date. This overview concludes with a critical survey of the various applications of the nanomaterials obtained from supramolecular cyclic peptide nanotubes, with a focus on biological and medical applications, ranging from ion channels and membrane insertion to antibacterial materials, anticancer drug delivery, gene delivery, and antiviral applications.

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“…The resulting macrodipole leads to exotic properties such as a significant piezoelectricity ( Tabata et al, 2019 ). Cyclic γ-amino acids ( cis -γ-aminocycloalkanecarboxylic acids, γ-Acas) of appropriate chirality, both alone ( Chen et al, 2020 ) or alternated with α-amino acids (α,γ-CPs), can also form nanotubes (α,γ-SCPNs) ( Amorín et al, 2003 ; Garcia-Fandino et al, 2012 ), where the β-carbon of the cycloalkane moiety is oriented toward the lumen of the cylinder, influencing the internal properties of the nanotube and opening the possibility of inner functionalization ( Figure 1A ). The first steps toward the preparation and characterization of α,γ-SCPNs with chemically functionalized lumens have already anticipated promising results in this area ( Reiriz et al, 2009 ; Calvelo et al, 2015 ; Rodríguez-Vázquez et al, 2017 ; Calvelo et al, 2019 ).…”

Section: Introductionmentioning

confidence: 99%

Transmembrane Self-Assembled Cyclic Peptide Nanotubes Based on α‐Residues and Cyclic δ‐Amino Acids: A Computational Study

et al. 2021

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Self-assembling cyclic peptide nanotubes have been shown to function as synthetic, integral transmembrane channels. The combination of natural and nonnatural aminoacids in the sequence of cyclic peptides enables the control not only of their outer surface but also of the inner cavity behavior and properties, affecting, for instance, their permeability to different molecules including water and ions. Here, a thorough computational study on a new class of self-assembling peptide motifs, in which δ-aminocycloalkanecarboxylic acids are alternated with natural α-amino acids, is presented. The presence of synthetic δ-residues creates hydrophobic regions in these α,δ-SCPNs, which makes them especially attractive for their potential implementation in the design of new drug or diagnostic agent carrier systems. Using molecular dynamics simulations, the behavior of water molecules, different ions (Li+, Na+, K+, Cs+, and Ca2+), and their correspondent counter Cl− anions is extensively investigated in the nanoconfined environment. The structure and dynamics are mutually combined in a diving immersion inside these transmembrane channels to discover a fascinating submarine nanoworld where star-shaped water channels guide the passage of cations and anions therethrough.

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Cyclic γ-Peptides With Transmembrane Water Channel Properties

Cited by 7 publications

References 38 publications

Inhibition of Ice Recrystallization by Nanotube-Forming Cyclic Peptides

Inhibition of Ice Recrystallization by Nanotube-Forming Cyclic Peptides

Molecular Self-Assembly and Supramolecular Chemistry of Cyclic Peptides

Transmembrane Self-Assembled Cyclic Peptide Nanotubes Based on α‐Residues and Cyclic δ‐Amino Acids: A Computational Study

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