Rational design of peptide nanotubes for varying diameters and lengths

Ueda, Mitsuru; Makino, Akihiro; Imai, Tomoya; Sugiyama, Junji; Kimura, Shunsaku

doi:10.1002/psc.1304

Cited by 48 publications

(64 citation statements)

References 27 publications

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“…36 In addition, it was shown that right-handed and left-handed amphiphilic helical peptides, containing 35-38 amino acids, were mixed to form peptide nanotubes with varying dimensions based on the helix-chirality of the peptides. 37 Yet, this approach is limited only to large peptide building blocks in which chirality could be induced. The challenge of controlling dipeptide nanotubes dimension in solution still remains without any solution so far.…”

mentioning

confidence: 99%

Controlling the Physical Dimensions of Peptide Nanotubes by Supramolecular Polymer Coassembly

Adler‐Abramovich¹,

Marco²,

Arnon³

et al. 2016

ACS Nano

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Molecular self-assembly of peptides into ordered nanotubes is highly important for various technological applications. Very short peptide building blocks, as short as dipeptides, can form assemblies with unique mechanical, optical, piezoelectric, and semiconductive properties. Yet, the control over nanotube length in solution has remained challenging, due to the inherent sequential self-assembly mechanism. Here, in line with polymer chemistry paradigms, we applied a supramolecular polymer coassembly methodology to modulate peptide nanotube elongation. Utilizing this approach, we achieved a narrow, controllable nanotube length distribution by adjusting the molecular ratio of the diphenylalanine assembly unit and its end-capped analogue. Kinetic analysis suggested a slower coassembly organization process as compared to the self-assembly dynamics of each of the building blocks separately. This is consistent with a hierarchal arrangement of the peptide moieties within the coassemblies. Mass spectrometry analysis demonstrated the bimolecular composition of the coassembled nanostructures. Moreover, the peptide nanotubes' length distribution, as determined by electron microscopy, was shown to fit a fragmentation kinetics model. Our results reveal a simple and efficient mechanism for the control of nanotube sizes through the coassembly of peptide entities at various ratios, allowing for the desired end-product formation. This dynamic size control offers tools for molecular engineering at the nanoscale exploiting the advantages of molecular coassembly.

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confidence: 99%

Controlling the Physical Dimensions of Peptide Nanotubes by Supramolecular Polymer Coassembly

Adler‐Abramovich¹,

Marco²,

Arnon³

et al. 2016

ACS Nano

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“…The degree of polymerization of poly(lactic acid) is 30, which length is long enough to take a helical structure . Aib‐based peptides have alternating sequences of Leu or Val and Aib residues, which also take α‐helical conformation . As previously reported, these molecular assemblies are formed on the basis of a tight molecular packing among helices, which allows precise control of vesicle diameters and membrane elasticity by choosing Leu or Val comprising helix and by combination of right‐handed and left‐handed helices …”

Section: Resultsmentioning

confidence: 89%

Modulation of immunogenicity of poly(sarcosine) displayed on various nanoparticle surfaces due to different physical properties

Kim

Hara

Watabe

et al. 2017

Journal of Peptide Science

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Poly(sarcosine) displayed on polymeric micelle is reported to trigger a T cell-independent type2 reaction with B1a cells in the mice to produce IgM and IgG3 antibodies. In addition to polymeric micelle, three kinds of vesicles displaying poly(sarcosine) on surface were prepared here to evaluate the amounts and avidities of IgM and IgG3, which were produced in mice, to correlate them with physical properties of the molecular assemblies. The largest amount of IgM was produced after twice administrations of a polymeric micelle of 35 nm diameter (G1). On the other hand, the production amount of IgG3 became the largest after twice administrations of G3 (vesicle of 229 nm diameter) or G4 (vesicle of 85 nm diameter). The augmented avidity of IgG3 after the twice administrations compared with that at the single administration was the highest with G3. These differences in immune responses are discussed in terms of surface density of poly(sarcosine) chains, nanoparticle size, hydrophobic component of poly(L-lactic acid) or (Leu- or Val-Aib) , and membrane elasticity of the nanoparticles. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.

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“…This area represents a fertile ground for research, as it will provide fundamental understanding of the interactions between polypeptoids and immune systems, which is critical for the further development of polypeptoid biomaterials for in vivo applications. poly(E-N-benzyloxycarbonyl-L-lysine), [99] poly(g-benzyl-L-glutamate), [99] poly(g-tert-butyl-L-glutamate), [100] and poly(S-ethylsulfonyl-L-cystine)], [101] PNMG-b-poly(E-caprolactone), [102] PNMG-b-poly[2-(3-butenyl)-2-oxazoline], [57] PNMG-b-(Leu-Aib) n [(Leu-Aib) n : helical peptides], [103][104][105][106][107][108][109][110] PNMG-b-poly(L-lactide) (AB, A 2 B, A 3 B types), [111] dextran-b-PNMG, [112] PEG-b-PNMG, [42] and C n512-18 -PNMG lipopolymers. [113][114][115] Their solution aggregation behavior has been reviewed by Luxenhofer et al [30] and will not be repeated here.…”

Section: Immunogenicitymentioning

confidence: 99%

Polypeptoid polymers: Synthesis, characterization, and properties

et al. 2017

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Polypeptoids, a class of peptidomimetic polymers, have emerged at the forefront of macromolecular and supramolecular science and engineering as the technological relevance of these polymers continues to be demonstrated. The chemical and structural diversity of polypeptoids have enabled access to and adjustment of a variety of physicochemical and biological properties (eg, solubility, charge characteristics, chain conformation, HLB, thermal processability, degradability, cytotoxicity and immunogenicity). These attributes have made this synthetic polymer platform a potential candidate for various biomedical and biotechnological applications. This review will provide an overview of recent development in synthetic methods to access polypeptoid polymers with well-defined structures and highlight some of the fundamental physicochemical and biological properties of polypeptoids that are pertinent to the future development of functional materials based on polypeptoids. | I N TR ODU C TI ONPolypeptoids composed of N-substituted polyglycine backbones are structural mimics of polypeptides ( Figure 1). Because of N-substitution, polypeptoids lack stereogenic centers and hydrogen bonding interactions along the main chains, in sharp contrast to polypeptides.As a result, the global conformations of polypeptoids are strongly dependent on the N-substituent structures, giving rise to random coils or well-defined secondary structures [eg, polyproline I (PPI) helix [1][2][3][4][5][6] and R-sheets] [7][8][9][10][11][12] that are reminiscent of those of polypeptides. The polypeptoid backbone containing tertiary amide linkages is highly polar and hydrophilic. The physicochemical properties of polypeptoids can be tailored by the N-substituent structures, enabling control over the hydrophilicity and lipophilicity balance (HLB), charge characteristics, [13,14] backbone conformation, [1][2][3][4][5][6][7][8][9][10][11][12] solubility, [15][16][17][18][19][20] thermal and crystallization properties of the polypeptoids. [21][22][23][24] Without extensive hydrogen bonding, polypeptoids are thermally processable similar to conventional thermoplastics, [20][21][22][23][24] whereas polypeptides undergo thermal degradation before they can be melt-processed due to the extensive hydrogen bonding interactions. While polypeptoids exhibited enhanced proteolytic stability relative to peptides, [25,26] they can be oxidatively degraded under conditions that mimic tissue inflammation, [27] suggesting their potential in vivo uses as biodegradable materials.Recent advances in the controlled polymerization methods have enabled access to a suite of structurally well-defined polypeptoids with various N-substituent structures and molecular architectures, setting the stage for the future development of polypeptoid materials for various targeted applications. Several review articles on the synthesis, properties, and application of polypeptoids for biomedical or nonbiomedical uses have been published in recent years. [28][29][30][31][32] As a result, this...

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Rational design of peptide nanotubes for varying diameters and lengths

Cited by 48 publications

References 27 publications

Controlling the Physical Dimensions of Peptide Nanotubes by Supramolecular Polymer Coassembly

Controlling the Physical Dimensions of Peptide Nanotubes by Supramolecular Polymer Coassembly

Modulation of immunogenicity of poly(sarcosine) displayed on various nanoparticle surfaces due to different physical properties

Polypeptoid polymers: Synthesis, characterization, and properties

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