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Special Issue "Self-Assembly Mechanism and Connection of Peptides and Proteins"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: closed (31 March 2021) | Viewed by 18143

Special Issue Editor

Prof. Dr. Kazunori Matsuura
E-Mail
Guest Editor
1. Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Koyama-Minami 4-101, Tottori 680-8552, Japan
2. Centre for Research on Green Sustainable Chemistry, Tottori University, Koyama-Minami 4-101, Tottori 680-8552, Japan
Interests: peptide chemistry; viral capsid; self-assembly; supramolecular chemistry; virus nanotechnology; liposome; DNA assembly; bio-imaging; microtubules

Special Issue Information

Dear Colleagues,

Self-assembly of rational designed peptides and peptide-protein conjugates enables the development of various bio-nanomaterials such as nanofibers, nanotubes, nanocapsules, and composite materials. Understanding the assembly/disassembly mechanism of the peptide/protein-based nanomaterials is important issue for the applications to drug carriers and scaffolds of cells. This special issue explores recent progress about self-assembly mechanism of peptides and peptide-protein conjugates used recent analytical methods such as microscopy, thermodynamic, and kinetic analyses

Prof. Kazunori Matsuura
Guest Editor

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Keywords

  • Self-assembly mechanism
  • Peptide
  • Peptide-protein conjugate
  • Nanofiber
  • Nanotube
  • Nanocapsule
  • Composite material
  • Microscopy
  • Thermodynamic analysis
  • Kinetic analysis

Published Papers (15 papers)

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Research

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Article
Fluorescence Correlation Spectroscopy Analysis of Effect of Molecular Crowding on Self-Assembly of β-Annulus Peptide into Artificial Viral Capsid
Int. J. Mol. Sci. 2021, 22(9), 4754; https://doi.org/10.3390/ijms22094754 - 30 Apr 2021
Cited by 1 | Viewed by 1118
Abstract
Recent progress in the de novo design of self-assembling peptides has enabled the construction of peptide-based viral capsids. Previously, we demonstrated that 24-mer β-annulus peptides from tomato bushy stunt virus spontaneously self-assemble into an artificial viral capsid. Here we propose to use [...] Read more.
Recent progress in the de novo design of self-assembling peptides has enabled the construction of peptide-based viral capsids. Previously, we demonstrated that 24-mer β-annulus peptides from tomato bushy stunt virus spontaneously self-assemble into an artificial viral capsid. Here we propose to use the artificial viral capsid through the self-assembly of β-annulus peptide as a simple model to analyze the effect of molecular crowding environment on the formation process of viral capsid. Artificial viral capsids formed by co-assembly of fluorescent-labelled and unmodified β-annulus peptides in dilute aqueous solutions and under molecular crowding conditions were analyzed using fluorescence correlation spectroscopy (FCS). The apparent particle size and the dissociation constant (Kd) of the assemblies decreased with increasing concentration of the molecular crowding agent, i.e., polyethylene glycol (PEG). This is the first successful in situ analysis of self-assembling process of artificial viral capsid under molecular crowding conditions. Full article
(This article belongs to the Special Issue Self-Assembly Mechanism and Connection of Peptides and Proteins)
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Article
Supramolecular Nanofibers from Collagen-Mimetic Peptides Bearing Various Aromatic Groups at N-Termini via Hierarchical Self-Assembly
Int. J. Mol. Sci. 2021, 22(9), 4533; https://doi.org/10.3390/ijms22094533 - 26 Apr 2021
Cited by 3 | Viewed by 864
Abstract
Self-assembly of artificial peptides has been widely studied for constructing nanostructured materials, with numerous potential applications in the nanobiotechnology field. Herein, we report the synthesis and hierarchical self-assembly of collagen-mimetic peptides (CMPs) bearing various aromatic groups at the N-termini, including 2-naphthyl, 1-naphtyl, [...] Read more.
Self-assembly of artificial peptides has been widely studied for constructing nanostructured materials, with numerous potential applications in the nanobiotechnology field. Herein, we report the synthesis and hierarchical self-assembly of collagen-mimetic peptides (CMPs) bearing various aromatic groups at the N-termini, including 2-naphthyl, 1-naphtyl, anthracenyl, and pyrenyl groups, into nanofibers. The CMPs (R-(GPO)n: n > 4) formed a triple helix structure in water at 4 °C, as confirmed via CD analyses, and their conformations were more stable with increasing hydrophobicity of the terminal aromatic group and peptide chain length. The resulting pre-organized triple helical CMPs showed diverse self-assembly into highly ordered nanofibers, reflecting their slight differences in hydrophobic/hydrophilic balance and configuration of aromatic templates. TEM analysis demonstrated that 2Np-CMPn (n = 6 and 7) and Py-CMP6 provided well-developed natural collagen-like nanofibers and An-CMPn (n = 5–7) self-assembled into rod-like micelle fibers. On the other hand, 2Np-CMP5 and 1Np-CMP6 were unable to form nanofibers under the same conditions. Furthermore, the Py-CMP6 nanofiber was found to encapsulate a guest hydrophobic molecule, Nile red, and exhibited unique emission behavior based on the specific nanostructure. In addition to the ability of CMPs to bind small molecules, their controlled self-assembly enables their versatile utilization in drug delivery and wavelength-conversion nanomaterials. Full article
(This article belongs to the Special Issue Self-Assembly Mechanism and Connection of Peptides and Proteins)
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Article
Thixotropic Hydrogels Composed of Self-Assembled Nanofibers of Double-Hydrophobic Elastin-Like Block Polypeptides
Int. J. Mol. Sci. 2021, 22(8), 4104; https://doi.org/10.3390/ijms22084104 - 15 Apr 2021
Cited by 3 | Viewed by 1178
Abstract
Physically crosslinked hydrogels with thixotropic properties attract considerable attention in the biomedical research field because their self-healing nature is useful in cell encapsulation, as injectable gels, and as bioinks for three-dimensional (3D) bioprinting. Here, we report the formation of thixotropic hydrogels containing nanofibers [...] Read more.
Physically crosslinked hydrogels with thixotropic properties attract considerable attention in the biomedical research field because their self-healing nature is useful in cell encapsulation, as injectable gels, and as bioinks for three-dimensional (3D) bioprinting. Here, we report the formation of thixotropic hydrogels containing nanofibers of double-hydrophobic elastin-like polypeptides (ELPs). The hydrogels are obtained with the double-hydrophobic ELPs at 0.5 wt%, the concentration of which is an order of magnitude lower than those for previously reported ELP hydrogels. Although the kinetics of hydrogel formation is slower for the double-hydrophobic ELP with a cell-binding sequence, the storage moduli G′ of mature hydrogels are similar regardless of the presence of a cell-binding sequence. Reversible gel–sol transitions are demonstrated in step-strain rheological measurements. The degree of recovery of the storage modulus G′ after the removal of high shear stress is improved by chemical crosslinking of nanofibers when intermolecular crosslinking is successful. This work would provide deeper insight into the structure–property relationships of the self-assembling polypeptides and a better design strategy for hydrogels with desired viscoelastic properties. Full article
(This article belongs to the Special Issue Self-Assembly Mechanism and Connection of Peptides and Proteins)
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Article
A Photoresponsive Artificial Viral Capsid Self-Assembled from an Azobenzene-Containing β-Annulus Peptide
Int. J. Mol. Sci. 2021, 22(8), 4028; https://doi.org/10.3390/ijms22084028 - 14 Apr 2021
Cited by 1 | Viewed by 1127
Abstract
Photoinduced structural changes in peptides can dynamically control the formation and dissociation of supramolecular peptide materials. However, the existence of photoresponsive viral capsids in nature remains unknown. In this study, we constructed an artificial viral capsid possessing a photochromic azobenzene moiety on the [...] Read more.
Photoinduced structural changes in peptides can dynamically control the formation and dissociation of supramolecular peptide materials. However, the existence of photoresponsive viral capsids in nature remains unknown. In this study, we constructed an artificial viral capsid possessing a photochromic azobenzene moiety on the peptide backbone. An azobenzene-containing β-annulus peptide derived from the tomato bushy stunt virus was prepared through solid-phase synthesis using Fmoc-3-[(3-aminomethyl)-phenylazo]phenylacetic acid. The azobenzene-containing β-annulus (β-Annulus-Azo) peptide showed a reversible trans/cis isomerization property. The β-annulus-azo peptide self-assembled at 25 μM into capsids with the diameters of 30–50 nm before UV irradiation (trans-form rich), whereas micrometer-sized aggregates were formed after UV irradiation (cis-form rich). The artificial viral capsid possessing azobenzene facilitated the encapsulation of fluorescent-labeled dextrans and their photoinduced release from the capsid. Full article
(This article belongs to the Special Issue Self-Assembly Mechanism and Connection of Peptides and Proteins)
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Article
pH-Responsive Self-Assembly of Designer Aromatic Peptide Amphiphiles and Enzymatic Post-Modification of Assembled Structures
Int. J. Mol. Sci. 2021, 22(7), 3459; https://doi.org/10.3390/ijms22073459 - 27 Mar 2021
Cited by 1 | Viewed by 1022
Abstract
Supramolecular fibrous materials in biological systems play important structural and functional roles, and therefore, there is a growing interest in synthetic materials that mimic such fibrils, especially those bearing enzymatic reactivity. In this study, we investigated the self-assembly and enzymatic post-modification of short [...] Read more.
Supramolecular fibrous materials in biological systems play important structural and functional roles, and therefore, there is a growing interest in synthetic materials that mimic such fibrils, especially those bearing enzymatic reactivity. In this study, we investigated the self-assembly and enzymatic post-modification of short aromatic peptide amphiphiles (PAs), Fmoc-LnQG (n = 2 or 3), which contain an LQG recognition unit for microbial transglutaminase (MTG). These aromatic PAs self-assemble into fibrous structures via π-π stacking interactions between the Fmoc groups and hydrogen bonds between the peptides. The intermolecular interactions and morphologies of the assemblies were influenced by the solution pH because of the change in the ionization states of the C-terminal carboxy group of the peptides. Moreover, MTG-catalyzed post-modification of a small fluorescent molecule bearing an amine group also showed pH dependency, where the enzymatic reaction rate was increased at higher pH, which may be because of the higher nucleophilicity of the amine group and the electrostatic interaction between MTG and the self-assembled Fmoc-LnQG. Finally, the accumulation of the fluorescent molecule on these assembled materials was directly observed by confocal fluorescence images. Our study provides a method to accumulate functional molecules on supramolecular structures enzymatically with the morphology control. Full article
(This article belongs to the Special Issue Self-Assembly Mechanism and Connection of Peptides and Proteins)
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Article
Synthesis and Self-Assembly Properties of Bola-Amphiphilic Glycosylated Lipopeptide-Type Supramolecular Hydrogels Showing Colour Changes Along with Gel–Sol Transition
Int. J. Mol. Sci. 2021, 22(4), 1860; https://doi.org/10.3390/ijms22041860 - 13 Feb 2021
Cited by 2 | Viewed by 1419
Abstract
Supramolecular hydrogels formed by self-assembly of low-molecular-weight amphiphiles (hydrogelators) have attracted significant attention, as smart and soft materials. However, most of the observed stimuli-responsive behaviour of these supramolecular hydrogels are limited to gel–sol transitions. In this study, we present bola-amphiphilic glycosylated lipopeptide-type supramolecular [...] Read more.
Supramolecular hydrogels formed by self-assembly of low-molecular-weight amphiphiles (hydrogelators) have attracted significant attention, as smart and soft materials. However, most of the observed stimuli-responsive behaviour of these supramolecular hydrogels are limited to gel–sol transitions. In this study, we present bola-amphiphilic glycosylated lipopeptide-type supramolecular hydrogelators that exhibit reversible thermochromism along with a gel–sol transition. The bola-amphiphiles have mono-, di-, tri- or tetra-phenylalanine (F) as a short peptide moiety. We investigate and discuss the effects of the number of F residues on the gelation ability and the morphology of the self-assembled nanostructures. Full article
(This article belongs to the Special Issue Self-Assembly Mechanism and Connection of Peptides and Proteins)
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Article
Design of RGDS Peptide-Immobilized Self-Assembling β-Strand Peptide from Barnacle Protein
Int. J. Mol. Sci. 2021, 22(3), 1240; https://doi.org/10.3390/ijms22031240 - 27 Jan 2021
Cited by 3 | Viewed by 797
Abstract
We designed three types of RGD-containing barnacle adhesive proteins using self-assembling peptides. In the present study, three types of RGD-containing peptides were synthesized by solid-phase peptide synthesis, and the secondary structures of these peptides were analyzed by CD and FT-IR spectroscopy. The mechanical [...] Read more.
We designed three types of RGD-containing barnacle adhesive proteins using self-assembling peptides. In the present study, three types of RGD-containing peptides were synthesized by solid-phase peptide synthesis, and the secondary structures of these peptides were analyzed by CD and FT-IR spectroscopy. The mechanical properties of peptide hydrogels were characterized by a rheometer. We discuss the correlation between the peptide conformation, and cell attachment and cell spreading activity from the viewpoint of developing effective tissue engineering scaffolds. We created a peptide-coated cell culture substrate by coating peptides on a polystyrene plate. They significantly facilitated cell adhesion and spreading compared to a non-coated substrate. When the RGDS sequence was modified at N- or C-terminal of R-Y, it was found that the self-assembling ability was dependent on the strongly affects hydrogel formation and cell adhesion caused by its secondary structure. Full article
(This article belongs to the Special Issue Self-Assembly Mechanism and Connection of Peptides and Proteins)
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Article
A Supramolecular Assembly of Hemoproteins Formed in a Star-Shaped Structure via Heme–Heme Pocket Interactions
Int. J. Mol. Sci. 2021, 22(3), 1012; https://doi.org/10.3390/ijms22031012 - 20 Jan 2021
Cited by 1 | Viewed by 1151
Abstract
Proteins have been used as building blocks to provide various supramolecular structures in efforts to develop nano-biomaterials possessing broad biological functionalities. A series of unique structures have been obtained from the engineering of hemoproteins which contain the iron porphyrin known as heme, as [...] Read more.
Proteins have been used as building blocks to provide various supramolecular structures in efforts to develop nano-biomaterials possessing broad biological functionalities. A series of unique structures have been obtained from the engineering of hemoproteins which contain the iron porphyrin known as heme, as a prosthetic group. This work in developing assembling systems is extended using cytochrome b562, a small electron transfer hemoprotein engineered to include an externally-attached heme moiety. The engineered units, which form a one-dimensional assembly via interprotein heme–heme pocket interactions, are conjugated to an apo-form of hexameric tyrosine-coordinated hemoprotein (apoHTHP) to provide a branching unit promoting the assembly of a star-shaped structure. The incorporation of the heme moiety attached to the protein surface of cytochrome b562 into apoHTHP can be accelerated by elevating the reaction temperature to generate a new assembly. The formation of a new larger assembly structure was confirmed by size exclusion chromatography. The ratio of the heme-containing units in the assemblies was analyzed by UV-Vis spectroscopy and the population of protein units estimated from SDS PAGE suggests the presence of plausible star-shaped structures, which are supported by hydrodynamic diameter data obtained by dynamic light scattering. Full article
(This article belongs to the Special Issue Self-Assembly Mechanism and Connection of Peptides and Proteins)
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Article
Protein Sensing Device with Multi-Recognition Ability Composed of Self-Organized Glycopeptide Bundle
Int. J. Mol. Sci. 2021, 22(1), 366; https://doi.org/10.3390/ijms22010366 - 31 Dec 2020
Cited by 2 | Viewed by 1044
Abstract
We designed and synthesized amphiphilic glycopeptides with glucose or galactose at the C-terminals. We observed the protein-induced structural changes of the amphiphilic glycopeptide assembly in the lipid bilayer membrane using transmission electron microscopy (TEM) and Fourier transform infrared reflection-absorption spectra (FTIR-RAS) measurements. [...] Read more.
We designed and synthesized amphiphilic glycopeptides with glucose or galactose at the C-terminals. We observed the protein-induced structural changes of the amphiphilic glycopeptide assembly in the lipid bilayer membrane using transmission electron microscopy (TEM) and Fourier transform infrared reflection-absorption spectra (FTIR-RAS) measurements. The glycopeptides re-arranged to form a bundle that acted as an ion channel due to the interaction among the target protein and the terminal sugar groups of the glycopeptides. The bundle in the lipid bilayer membrane was fixed on a gold-deposited quartz crystal microbalance (QCM) electrode by the membrane fusion method. The protein-induced re-arrangement of the terminal sugar groups formed a binding site that acted as a receptor, and the re-binding of the target protein to the binding site induced the closing of the channel. We monitored the detection of target proteins by the changes of the electrochemical properties of the membrane. The response current of the membrane induced by the target protein recognition was expressed by an equivalent circuit consisting of resistors and capacitors when a triangular voltage was applied. We used peanut lectin (PNA) and concanavalin A (ConA) as target proteins. The sensing membrane induced by PNA shows the specific response to PNA, and the ConA-induced membrane responded selectively to ConA. Furthermore, PNA-induced sensing membranes showed relatively low recognition ability for lectin from Ricinus Agglutinin (RCA120) and mushroom lectin (ABA), which have galactose binding sites. The protein-induced self-organization formed the spatial arrangement of the sugar chains specific to the binding site of the target protein. These findings demonstrate the possibility of fabricating a sensing device with multi-recognition ability that can recognize proteins even if the structure is unknown, by the protein-induced self-organization process. Full article
(This article belongs to the Special Issue Self-Assembly Mechanism and Connection of Peptides and Proteins)
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Article
Peptide-Mediated Gene Transfer into Marine Purple Photosynthetic Bacteria
Int. J. Mol. Sci. 2020, 21(22), 8625; https://doi.org/10.3390/ijms21228625 - 16 Nov 2020
Cited by 1 | Viewed by 916
Abstract
Use of photosynthetic organisms is one of the sustainable ways to produce high-value products. Marine purple photosynthetic bacteria are one of the research focuses as microbial production hosts. Genetic transformation is indispensable as a biotechnology technique. However, only conjugation has been determined to [...] Read more.
Use of photosynthetic organisms is one of the sustainable ways to produce high-value products. Marine purple photosynthetic bacteria are one of the research focuses as microbial production hosts. Genetic transformation is indispensable as a biotechnology technique. However, only conjugation has been determined to be an applicable method for the transformation of marine purple photosynthetic bacteria so far. In this study, for the first time, a dual peptide-based transformation method combining cell penetrating peptide (CPP), cationic peptide and Tat-derived peptide (dTat-Sar-EED) (containing D-amino acids of Tat and endosomal escape domain (EED) connected by sarcosine linkers) successfully delivered plasmid DNA into Rhodovulum sulfidophilum, a marine purple photosynthetic bacterium. The plasmid delivery efficiency was greatly improved by dTat-Sar-EED. The concentrations of dTat-Sar-EED, cell growth stage and recovery duration affected the efficiency of plasmid DNA delivery. The delivery was inhibited at 4 °C and by A22, which is an inhibitor of the actin homolog MreB. This suggests that the plasmid DNA delivery occurred via MreB-mediated energy dependent process. Additionally, this peptide-mediated delivery method was also applicable for E. coli cells. Thus, a wide range of bacteria could be genetically transformed by using this novel peptide-based transformation method. Full article
(This article belongs to the Special Issue Self-Assembly Mechanism and Connection of Peptides and Proteins)
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Article
Selective Gold Recovery from Homogenous Aqueous Solutions Containing Gold and Platinum Ions by Aromatic Amino Acid-Containing Peptides
Int. J. Mol. Sci. 2020, 21(14), 5060; https://doi.org/10.3390/ijms21145060 - 17 Jul 2020
Cited by 3 | Viewed by 943
Abstract
There is increasing interest in the development of noble metal separation/recovery processes, especially for applications to “urban mining”. Common separation/recovery processes for noble metals use a solvent (liquid-liquid) extraction technique in hydrometallurgy. However, these processes are time-consuming and not environmentally friendly, because they [...] Read more.
There is increasing interest in the development of noble metal separation/recovery processes, especially for applications to “urban mining”. Common separation/recovery processes for noble metals use a solvent (liquid-liquid) extraction technique in hydrometallurgy. However, these processes are time-consuming and not environmentally friendly, because they use organic solvents for sequential metal ion extractions. Electrowinning is an alternative approach for selective metal precipitation that involves controlling the redox potentials of electrodes but requires specialized equipment and generates hydrogen as a byproduct at the cathode surface under dilute conditions. In the present study, we investigated selective gold recovery from a homogenous aqueous solution containing a mixture of dilute HAuCl4 and H2PtCl6 (5.0 × 10−5 M each) and aromatic amino acid-containing peptides (2.0 × 10−4 M each). Gold selectivity was determined by analyzing the compositions of the solids and supernatants obtained from the reaction mixtures. A much higher gold selectivity (gold/platinum (Au/Pt) atomic ratio = 7.5) was obtained using an anthracene-containing peptide compared to peptides containing one or two naphthalene ring(s). Our proposed approach is applicable to the sequential separation of several noble metal ions, such as Au, palladium (Pd), Pt, iridium (Ir) and rhodium (Rh), and simply requires developing aromatics suitable for each noble metal of interest. Full article
(This article belongs to the Special Issue Self-Assembly Mechanism and Connection of Peptides and Proteins)
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Review

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Review
Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils
Int. J. Mol. Sci. 2021, 22(9), 4349; https://doi.org/10.3390/ijms22094349 - 21 Apr 2021
Cited by 11 | Viewed by 1303
Abstract
Amyloid fibrils are supramolecular protein assemblies represented by a cross-β structure and fibrous morphology, whose structural architecture has been previously investigated. While amyloid fibrils are basically a main-chain-dominated structure consisting of a backbone of hydrogen bonds, side-chain interactions also play an important role [...] Read more.
Amyloid fibrils are supramolecular protein assemblies represented by a cross-β structure and fibrous morphology, whose structural architecture has been previously investigated. While amyloid fibrils are basically a main-chain-dominated structure consisting of a backbone of hydrogen bonds, side-chain interactions also play an important role in determining their detailed structures and physicochemical properties. In amyloid fibrils comprising short peptide segments, a steric zipper where a pair of β-sheets with side chains interdigitate tightly is found as a fundamental motif. In amyloid fibrils comprising longer polypeptides, each polypeptide chain folds into a planar structure composed of several β-strands linked by turns or loops, and the steric zippers are formed locally to stabilize the structure. Multiple segments capable of forming steric zippers are contained within a single protein molecule in many cases, and polymorphism appears as a result of the diverse regions and counterparts of the steric zippers. Furthermore, the β-solenoid structure, where the polypeptide chain folds in a solenoid shape with side chains packed inside, is recognized as another important amyloid motif. While side-chain interactions are primarily achieved by non-polar residues in disease-related amyloid fibrils, the participation of hydrophilic and charged residues is prominent in functional amyloids, which often leads to spatiotemporally controlled fibrillation, high reversibility, and the formation of labile amyloids with kinked backbone topology. Achieving precise control of the side-chain interactions within amyloid structures will open up a new horizon for designing useful amyloid-based nanomaterials. Full article
(This article belongs to the Special Issue Self-Assembly Mechanism and Connection of Peptides and Proteins)
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Review
The Versatile Manipulations of Self-Assembled Proteins in Vaccine Design
Int. J. Mol. Sci. 2021, 22(4), 1934; https://doi.org/10.3390/ijms22041934 - 16 Feb 2021
Cited by 10 | Viewed by 1476
Abstract
Protein assemblies provide unique structural features which make them useful as carrier molecules in biomedical and chemical science. Protein assemblies can accommodate a variety of organic, inorganic and biological molecules such as small proteins and peptides and have been used in development of [...] Read more.
Protein assemblies provide unique structural features which make them useful as carrier molecules in biomedical and chemical science. Protein assemblies can accommodate a variety of organic, inorganic and biological molecules such as small proteins and peptides and have been used in development of subunit vaccines via display parts of viral pathogens or antigens. Such subunit vaccines are much safer than traditional vaccines based on inactivated pathogens which are more likely to produce side-effects. Therefore, to tackle a pandemic and rapidly produce safer and more effective subunit vaccines based on protein assemblies, it is necessary to understand the basic structural features which drive protein self-assembly and functionalization of portions of pathogens. This review highlights recent developments and future perspectives in production of non-viral protein assemblies with essential structural features of subunit vaccines. Full article
(This article belongs to the Special Issue Self-Assembly Mechanism and Connection of Peptides and Proteins)
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Review
Supramolecular Architectures of Nucleic Acid/Peptide Hybrids
Int. J. Mol. Sci. 2020, 21(24), 9458; https://doi.org/10.3390/ijms21249458 - 12 Dec 2020
Cited by 4 | Viewed by 1345
Abstract
Supramolecular architectures that are built artificially from biomolecules, such as nucleic acids or peptides, with structural hierarchical orders ranging from the molecular to nano-scales have attracted increased attention in molecular science research fields. The engineering of nanostructures with such biomolecule-based supramolecular architectures could [...] Read more.
Supramolecular architectures that are built artificially from biomolecules, such as nucleic acids or peptides, with structural hierarchical orders ranging from the molecular to nano-scales have attracted increased attention in molecular science research fields. The engineering of nanostructures with such biomolecule-based supramolecular architectures could offer an opportunity for the development of biocompatible supramolecular (nano)materials. In this review, we highlighted a variety of supramolecular architectures that were assembled from both nucleic acids and peptides through the non-covalent interactions between them or the covalently conjugated molecular hybrids between them. Full article
(This article belongs to the Special Issue Self-Assembly Mechanism and Connection of Peptides and Proteins)
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Review
Current Progress in Cross-Linked Peptide Self-Assemblies
Int. J. Mol. Sci. 2020, 21(20), 7577; https://doi.org/10.3390/ijms21207577 - 14 Oct 2020
Cited by 8 | Viewed by 1426
Abstract
Peptide-based fibrous supramolecular assemblies represent an emerging class of biomaterials that can realize various bioactivities and structures. Recently, a variety of peptide fibers with attractive functions have been designed together with the discovery of many peptide-based self-assembly units. Cross-linking of the peptide fibers [...] Read more.
Peptide-based fibrous supramolecular assemblies represent an emerging class of biomaterials that can realize various bioactivities and structures. Recently, a variety of peptide fibers with attractive functions have been designed together with the discovery of many peptide-based self-assembly units. Cross-linking of the peptide fibers is a key strategy to improve the functions of these materials. The cross-linking of peptide fibers forming three-dimensional networks in a dispersion can lead to changes in physical and chemical properties. Hydrogelation is a typical change caused by cross-linking, which makes it applicable to biomaterials such as cell scaffold materials. Cross-linking methods, which have been conventionally developed using water-soluble covalent polymers, are also useful in supramolecular peptide fibers. In the case of peptide fibers, unique cross-linking strategies can be designed by taking advantage of the functions of amino acids. This review focuses on the current progress in the design of cross-linked peptide fibers and their applications. Full article
(This article belongs to the Special Issue Self-Assembly Mechanism and Connection of Peptides and Proteins)
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