Peptide α-helices for synthetic nanostructures

2007 ◽  
Vol 35 (3) ◽  
pp. 487-491 ◽  
Author(s):  
M.G. Ryadnov

Supramolecular structures arising from a broad range of chemical archetypes are of great technological promise. Defining such structures at the nanoscale is crucial to access principally new types of functional materials for applications in bionanotechnology. In this vein, biomolecular self-assembly has emerged as an efficient approach for building synthetic nanostructures from the bottom up. The approach predominantly employs the spontaneous folding of biopolymers to monodisperse three-dimensional shapes that assemble into hierarchically defined mesoscale composites. An immediate interest here is the extraction of reliable rules that link the chemistry of biopolymers to the mechanisms of their assembly. Once established these can be further harnessed in designing supramolecular objects de novo. Different biopolymer classes compile a rich repertoire of assembly motifs to facilitate the synthesis of otherwise inaccessible nanostructures. Among those are peptide α-helices, ubiquitous folding elements of natural protein assemblies. These are particularly appealing candidates for prescriptive supramolecular engineering, as their well-established and conservative design rules give unmatched predictability and rationale. Recent developments of self-assembling systems based on helical peptides, including fibrous systems, nanoscale linkers and reactors will be highlighted herein.

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Fengbin Wang ◽  
Ordy Gnewou ◽  
Charles Modlin ◽  
Leticia C. Beltran ◽  
Chunfu Xu ◽  
...  

AbstractThe exquisite structure-function correlations observed in filamentous protein assemblies provide a paradigm for the design of synthetic peptide-based nanomaterials. However, the plasticity of quaternary structure in sequence-space and the lability of helical symmetry present significant challenges to the de novo design and structural analysis of such filaments. Here, we describe a rational approach to design self-assembling peptide nanotubes based on controlling lateral interactions between protofilaments having an unusual cross-α supramolecular architecture. Near-atomic resolution cryo-EM structural analysis of seven designed nanotubes provides insight into the designability of interfaces within these synthetic peptide assemblies and identifies a non-native structural interaction based on a pair of arginine residues. This arginine clasp motif can robustly mediate cohesive interactions between protofilaments within the cross-α nanotubes. The structure of the resultant assemblies can be controlled through the sequence and length of the peptide subunits, which generates synthetic peptide filaments of similar dimensions to flagella and pili.


2020 ◽  
Vol 7 (8) ◽  
pp. 200642
Author(s):  
Syed Kumail Abbas ◽  
Ghulam M. Mustafa ◽  
Murtaza Saleem ◽  
Muhammad Sufyan ◽  
Saira Riaz ◽  
...  

Controlled growth of nanostructures plays a vital role in tuning the physical and chemical properties of functional materials for advanced energy and memory storage devices. Herein, we synthesized hierarchical micro-sized flowers, built by the self-assembly of highly crystalline, two-dimensional nanoplates of Co- and Ni-doped BiFeO 3 , using a simple ethylene glycol-mediated solvothermal method. Pure BiFeO 3 attained scattered one-dimensional nanorods-type morphology having diameter nearly 60 nm. Co-doping of Co and Ni at Fe-site in BiFeO 3 does not destabilize the morphology; rather it generates three-dimensional floral patterns of self-assembled nanoplates. Unsaturated polarization loops obtained for BiFeO 3 confirmed the leakage behaviour of these rhombohedrally distorted cubic perovskites. These loops were then used to determine the energy density of the BiFeO 3 perovskites. Enhanced ferromagnetic behaviour with high coercivity and remanence was observed for these nanoplates. A detailed discussion about the origin of ferromagnetic behaviour based on Goodenough–Kanamori's rule is also a part of this paper. Impedance spectroscopy revealed a true Warburg capacitive behaviour of the synthesized nanoplates. High magneto-electric (ME) coefficient of 27 mV cm −1 Oe −1 at a bias field of −0.2 Oe was observed which confirmed the existence of ME coupling in these nanoplates.


2019 ◽  
Vol 21 (21) ◽  
pp. 10879-10883 ◽  
Author(s):  
Yumi Ozawa ◽  
Hisako Sato ◽  
Yohei Kayano ◽  
Nana Yamaki ◽  
Yu-ichiro Izato ◽  
...  

Self-assembling phenylalanine-based peptides have garnered interest owing to their potential for creating new functional materials. l-Phe-l-Phe-d-Phe tripeptide forms a γ-turn structure in the nanostructure.


2020 ◽  
Vol 6 (24) ◽  
pp. eaaz7202 ◽  
Author(s):  
Bijal B. Patel ◽  
Dylan J. Walsh ◽  
Do Hoon Kim ◽  
Justin Kwok ◽  
Byeongdu Lee ◽  
...  

Additive manufacturing of functional materials is limited by control of microstructure and assembly at the nanoscale. In this work, we integrate nonequilibrium self-assembly with direct-write three-dimensional (3D) printing to prepare bottlebrush block copolymer (BBCP) photonic crystals (PCs) with tunable structure color. After varying deposition conditions during printing of a single ink solution, peak reflected wavelength for BBCP PCs span a range of 403 to 626 nm (blue to red), corresponding to an estimated change in d-spacing of >70 nm (Bragg- Snell equation). Physical characterization confirms that these vivid optical effects are underpinned by tuning of lamellar domain spacing, which we attribute to modulation of polymer conformation. Using in situ optical microscopy and solvent-vapor annealing, we identify kinetic trapping of metastable microstructures during printing as the mechanism for domain size control. More generally, we present a robust processing scheme with potential for on-the-fly property tuning of a variety of functional materials.


Nanomaterials ◽  
2020 ◽  
Vol 10 (5) ◽  
pp. 1008 ◽  
Author(s):  
Ximena Zottig ◽  
Mélanie Côté-Cyr ◽  
Dominic Arpin ◽  
Denis Archambault ◽  
Steve Bourgault

Life-inspired protein supramolecular assemblies have recently attracted considerable attention for the development of next-generation vaccines to fight against infectious diseases, as well as autoimmune diseases and cancer. Protein self-assembly enables atomic scale precision over the final architecture, with a remarkable diversity of structures and functionalities. Self-assembling protein nanovaccines are associated with numerous advantages, including biocompatibility, stability, molecular specificity and multivalency. Owing to their nanoscale size, proteinaceous nature, symmetrical organization and repetitive antigen display, protein assemblies closely mimic most invading pathogens, serving as danger signals for the immune system. Elucidating how the structural and physicochemical properties of the assemblies modulate the potency and the polarization of the immune responses is critical for bottom-up design of vaccines. In this context, this review briefly covers the fundamentals of supramolecular interactions involved in protein self-assembly and presents the strategies to design and functionalize these assemblies. Examples of advanced nanovaccines are presented, and properties of protein supramolecular structures enabling modulation of the immune responses are discussed. Combining the understanding of the self-assembly process at the molecular level with knowledge regarding the activation of the innate and adaptive immune responses will support the design of safe and effective nanovaccines.


RSC Advances ◽  
2014 ◽  
Vol 4 (91) ◽  
pp. 49780-49782 ◽  
Author(s):  
Fan Wu ◽  
Yuan Wang ◽  
Mingyang Wang

A novel self-assembling 3D-RGO/PEDOT architecture has been synthesized through organic solvent absorption and gentle heating. It gives a promising application in electromagnetic absorption.


Molecules ◽  
2020 ◽  
Vol 25 (13) ◽  
pp. 2995 ◽  
Author(s):  
Tiziano Carlomagno ◽  
Maria C. Cringoli ◽  
Slavko Kralj ◽  
Marina Kurbasic ◽  
Paolo Fornasiero ◽  
...  

Self-assembling peptides are attracting wide interest as biodegradable building blocks to achieve functional nanomaterials that do not persist in the environment. Amongst the many applications, biocatalysis is gaining momentum, although a clear structure-to-activity relationship is still lacking. This work applied emerging design rules to the heterochiral octapeptide sequence His–Leu–DLeu–Ile–His–Leu–DLeu–Ile for self-assembly into nanofibrils that, at higher concentration, give rise to a supramolecular hydrogel for the mimicry of esterase-like activity. The peptide was synthesized by solid-phase and purified by HPLC, while its identity was confirmed by 1H-NMR and electrospray ionization (ESI)-MS. The hydrogel formed by this peptide was studied with oscillatory rheometry, and the supramolecular behavior of the peptide was investigated with transmission electron microscopy (TEM) analysis, circular dichroism (CD) spectroscopy, thioflavin T amyloid fluorescence assay, and attenuated total reflectance (ATR) Fourier-transform infrared (FT-IR) spectroscopy. The biocatalytic activity was studied by monitoring the hydrolysis of p-nitrophenyl acetate (pNPA) at neutral pH, and the reaction kinetics followed an apparent Michaelis–Menten model, for which a Lineweaver–Burk plot was produced to determine its enzymatic parameters for a comparison with the literature. Finally, LC–MS analysis was conducted on a series of experiments to evaluate the extent of, if any, undesired peptide acetylation at the N-terminus. In conclusion, we provide new insights that allow gaining a clearer picture of self-assembling peptide design rules for biocatalysis.


2012 ◽  
Vol 40 (4) ◽  
pp. 629-634 ◽  
Author(s):  
Tibor Doles ◽  
Sabina Božič ◽  
Helena Gradišar ◽  
Roman Jerala

Bionanotechnology seeks to modify and design new biopolymers and their applications and uses biological systems as cell factories for the production of nanomaterials. Molecular self-assembly as the main organizing principle of biological systems is also the driving force for the assembly of artificial bionanomaterials. Protein domains and peptides are particularly attractive as building blocks because of their ability to form complex three-dimensional assemblies from a combination of at least two oligomerization domains that have the oligomerization state of at least two and three respectively. In the present paper, we review the application of polypeptide-based material for the formation of material with nanometre-scale pores that can be used for the separation. Use of antiparallel coiled-coil dimerization domains introduces the possibility of modulation of pore size and chemical properties. Assembly or disassembly of bionanomaterials can be regulated by an external signal as demonstrated by the coumermycin-induced dimerization of the gyrase B domain which triggers the formation of polypeptide assembly.


2014 ◽  
Vol 1706 ◽  
Author(s):  
Hiroaki Wakayama ◽  
Hirotaka Yonekura ◽  
Yasuaki Kawai

ABSTRACTPeriodically ordered nanohetero inorganic structures offer great promise due to their unique electric, ionic, magnetic, and photonic properties. Many studies have focused on the formation of periodically ordered nano-hetero inorganic structures through layer-by-layer adsorption, sputtering, and self-assembly methods. However, the construction of three-dimensional periodically ordered nanohetero inorganic structures with desired sizes and morphologies remains a great challenge. We present a simple method for producing three-dimensional periodically ordered inorganic nanoheterostructures with controlled shape and size by replicating self-assembled block copolymers (BCPs) containing precursors of metals and metal oxides. Precursors were dissolved with BCPs in a solvent. Upon evaporation of the solvent, each precursor was selectively introduced into a separate polymer block. Application of an external magnetic field (10 T) to the BCP-precursor composites resulted in a phase transition of from spheres to hexagonal cylinders. Subsequent pyrolytic removal of the BCPs produced periodically ordered nanoheterostructures that were structural replicates of the precursor–BCP composites. Self-assembled nano-hetero inorganic structures of nanoparticles, nanorods and layers in a matrix were produced. The morphology and domain size can be tailored by controlling the molecular weight and relative block length of block copolymers. The controlled size and morphology of the inorganic nanoheterostructures demonstrate the method’s utility for producing highly functional materials.


2007 ◽  
Vol 86 (5) ◽  
pp. 426-430 ◽  
Author(s):  
J. Kirkham ◽  
A. Firth ◽  
D. Vernals ◽  
N. Boden ◽  
C. Robinson ◽  
...  

Rationally designed β-sheet-forming peptides that spontaneously form three-dimensional fibrillar scaffolds in response to specific environmental triggers may potentially be used in skeletal tissue engineering, including the treatment/prevention of dental caries, via bioactive surface groups. We hypothesized that infiltration of caries lesions with monomeric low-viscosity peptide solutions would be followed by in situ polymerization triggered by conditions of pH and ionic strength, providing a biomimetic scaffold capable of hydroxyapatite nucleation, promoting repair. Our aim was to determine the effect of an anionic peptide applied to caries-like lesions in human dental enamel under simulated intra-oral conditions of pH cycling. Peptide treatment significantly increased net mineral gain by the lesions, due to both increased remineralization and inhibition of demineralization over a five-day period. The assembled peptide was also capable of inducing hydroxyapatite nucleation de novo. The results suggest that self-assembling peptides may be useful in the modulation of mineral behavior during in situ dental tissue engineering.


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