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2007, Macromolecular Bioscience
Molecular self-assembly is ubiquitous in Nature, from lipids that form oil droplets in water, and surfactants that form micelles and other complex structures in water, to sophisticated multiunit ribosome and virus assemblies. Nature is a grand master who utilizes the strategy to bottom-up build hierarchical materials. These elegant molecular self-assembly systems lie at the interface between biochemistry, molecular biology, peptide and protein chemistry, macromolecular science, materials science, and engineering. The key elements are chemical
culturing and energy materials . The mechanical properties of organogels are the key technique problems that needed to improve for applications.
Chemical Society Reviews
Nature is enriched with a wide variety of complex, synergistic and highly functional protein-based multicomponent assemblies.
Handbook of Nanomaterials Properties, 2014
Organic & Biomolecular Chemistry, 2014
The formation of well-ordered nanostructures through self-assembly of diverse organic and inorganic building blocks has drawn much attention owing to their potential applications in biology and chemistry.
Wiley Interdisciplinary Reviews: Nanomedicine and Nanobiotechnology, 2013
Self-assembly is a ubiquitous process in biology where it plays numerous important roles and underlies the formation of a wide variety of complex biological structures. Over the past two decades, materials scientists have aspired to exploit nature's assembly principles to create artificial materials, with hierarchical structures and tailored properties, for the fabrication of functional devices. Toward this goal, both biological and synthetic building blocks have been subject of extensive research in self-assembly. In fact, molecular self-assembly is becoming increasingly important for the fabrication of biomaterials because it offers a great platform for constructing materials with high level of precision and complexity, integrating order and dynamics, to achieve functions such as stimuliresponsiveness, adaptation, recognition, transport, and catalysis. The importance of peptide self-assembling building blocks has been recognized in the last years, as demonstrated by the literature available on the topic. The simple structure of peptides, as well as their facile synthesis, makes peptides an excellent family of structural units for the bottom-up fabrication of complex nanobiomaterials. Additionally, peptides offer a great diversity of biochemical (specificity, intrinsic bioactivity, biodegradability) and physical (small size, conformation) properties to form self-assembled structures with different molecular configurations. The motivation of this review is to provide an overview on the design principles for peptide self-assembly and to illustrate how these principles have been applied to manipulate their self-assembly across the scales. Applications of self-assembling peptides as nanobiomaterials, including carriers for drug delivery, hydrogels for cell culture and tissue repair are also described.
2024
Peptides have tremendous potential as building blocks of designer materials with wideranging applications. These materials are stabilized by strongly directional hydrogen bonding patterns giving rise to one-, or two-dimensional assembly. It remains a challenge to mimic biology's context-adaptive and flexible structures. Here, we introduce minimalistic tripeptide sequences that form dynamic ensembles through incorporation of multivalent sidechain interactions that collectively self-optimize depending on their context. Notably, we observed that these dispersions undergo drying-induced liquid to solid phase separation involving interface stabilization and expansion, resulting in formation of films of stiff, and densely packed, porous peptide microparticles that can be instantaneously redispersed upon re-introduction of water. Airdrying of aqueous peptide dispersions in the presence of proteins or small molecule payloads results in spontaneous and efficient encapsulation, and retention of protein stability after redispersion. These supramolecular tripeptide dispersions show promise for emulsification, encapsulation, and storage of biomacromolecules.
2011
In this study, we perform a morphological evaluation of the diverse nanostructures formed by varying concentration and amino acid sequence of a unique class of ultrasmall self-assembling peptides. We modified these peptides by replacing the aliphatic amino acid at the C-aliphatic terminus with different aromatic amino acids. We tracked the effect of introducing aromatic residues on self-assembly and morphology of resulting nanostructures. Whereas aliphatic peptides formed long, helical fibers that entangle into meshes and entrap >99.9% water, the modified peptides contrastingly formed short, straight fibers with a flat morphology. No helical fibers were observed for the modified peptides. For the aliphatic peptides at low concentrations, different supramolecular assemblies such as hollow nanospheres and membrane blebs were found. Since the ultrasmall peptides are made of simple, aliphatic amino acids, considered to have existed in the primordial soup, study of these supramolecular assemblies could be relevant to understanding chemical evolution leading to the origin of life on Earth. In particular, we propose a variety of potential applications in bioengineering and nanotechnology for the diverse self-assembled nanostructures.
Chem
This work explains why and how heterochiral and homochiral tripeptides differ in their assembly in water. A characteristic spectroscopic signature is assigned to molecular conformation. We monitor the process as a continuum from the molecular scale to the macroscopic biomaterials so that the final properties are linked to chemical structure of the building blocks. This work lays the foundation for the design of supramolecular hydrogel biomaterials based on short sequences of hydrophobic D-and L-amino acids.
Methods in molecular biology (Clifton, N.J.), 2017
In recent years there has been increasing interest in nanostructure design based on the self-assembly properties of proteins and polymers. Nanodesign requires the ability to predictably manipulate the properties of the self-assembly of autonomous building blocks, which can fold or aggregate into preferred conformational states. The design includes functional synthetic materials and biological macromolecules. Autonomous biological building blocks with available 3D structures provide an extremely rich and useful resource. Structural databases contain large libraries of protein molecules and their building blocks with a range of sizes, shapes, surfaces, and chemical properties. The introduction of engineered synthetic residues or short peptides into these building blocks can greatly expand the available chemical space and enhance the desired properties. Herein, we summarize a protocol for designing nanostructures consisting of self-assembling building blocks, based on our recent works....
2017
Self-assembling building blocks have become of increasing interest in the field of bionanotechnology due to their ability to self-assemble into defined geometrical shapes. Nature is abundant with examples of functional biological assemblies that are either rich in β-sheets or coiled coils. This research work investigates peptide sequences derived from simple protein interfaces, as molecular tectons for use in bionanotechnology. Protein interface sequences were chosen as a design source of peptide tectons, as they are naturally optimized to drive self-assembly in a highly controlled and regulated manner. This thesis work focused primarily on the simple β-continuous and the helical coiled coil protein interfaces. The peptide sequences designed from different protein-β interfaces all self-assembled into well-ordered nanostructures that were β-sheet rich and exhibited liquid crystallinity. SAXS and FTIR confirmed that the extended peptide nanostructures have the common architecture of β...
OnLine Journal of Biological Sciences
Self-assembling of peptides is a spontaneous process by which peptides are self-organized to form well-ordered structures by intramolecular and intermolecular interactions. This process is controlled by the balance of the forces (attractive and repulsive) within the peptide molecules. Notable methods used for the synthesis of self-assembly peptides are solid-phase synthesis, liquid-phase synthesis, recombinant technology, and the use of external fields. The self-assembled nanostructure-based peptides offer remarkable advantages; such as mild synthesis conditions, relatively simple functionalization, fast synthesis, and low cost, resulting in their remarkable potential for use in biosensors, imaging tools, antimicrobial agents, drug delivery systems, bioelectronics, tissue reparation. Herein, we present the origin of self-assembled peptides, synthesis of novel materials produced through self-assembly of peptides, structural elucidation, applications, recent trends, and the future outlook of self-assembly peptides.
In this tutorial review the process and applications of peptide self-assembly into nanotubes, nanospheres, nanofibrils, nanotapes, and other ordered structures at the nano-scale are discussed. The formation of well-ordered nanostructures by a process of self-association represents the essence of modern nanotechnology. Such self-assembled structures can be formed by a variety of building blocks, both organic and inorganic. Of the organic building blocks, peptides are among the most useful ones. Peptides possess the biocompatibility and chemical diversity that are found in proteins, yet they are much more stable and robust and can be readily synthesized on a large scale. Short peptides can spontaneously associate to form nanotubes, nanospheres, nanofibrils, nanotapes, and other ordered structures at the nano-scale. Peptides can also form macroscopic assemblies such as hydrogels with nano-scale order. The application of peptide building blocks in biosensors, tissue engineering, and the development of antibacterial agents has already been demonstrated.
Trends in Biotechnology, 2007
Self-assembly at the nanoscale is becoming increasingly important for the fabrication of novel supramolecular structures, with applications in the fields of nanobiotechnology and nanomedicine. Peptides represent the most favorable building blocks for the design and synthesis of nanostructures because they offer a great diversity of chemical and physical properties, they can be synthesized in large amounts, and can be modified and decorated with functional elements, which can be used in diverse applications. In this article, we review some of the most recent experimental advances in the use of nanoscale self-assembled peptide structures and the theoretical efforts aimed at understanding the microscopic determinants of their formation, stability and conformational properties. The combination of experimental observations and theoretical advances will be fundamental to fully realizing the biotechnological potential of peptide self-organization.
Angewandte Chemie, 2021
Herein, we report the rich morphological and conformational versatility of a biologically active peptide (PEP-1), which follows diverse self-assembly pathways to form up to six distinct nanostructures and up to four different secondary structures through subtle modulation in pH, concentration and temperature. PEP-1 forms twisted b-sheet secondary structures and nanofibers at pH 7.4, which transform into fractal-like structures with strong b-sheet conformations at pH 13.0 or short disorganized elliptical aggregates at pH 5.5. Upon dilution at pH 7.4, the nanofibers with twisted bsheet secondary structural elements convert into nanoparticles with random coil conformations. Interestingly, these two selfassembled states at pH 7.4 and room temperature are kinetically controlled and undergo a further transformation into thermodynamically stable states upon thermal annealing: whereas the twisted b-sheet structures and corresponding nanofibers transform into 2D sheets with well-defined b-sheet domains, the nanoparticles with random coil structures convert into short nanorods with a-helix conformations. Notably, PEP-1 also showed high biocompatibility, low hemolytic activity and marked antibacterial activity, rendering our system a promising candidate for multiple bio-applications.
Nanomaterials, 2022
Self-assembly is the most suitable approach to obtaining peptide-based materials on the nano- and mesoscopic scales. Applications span from peptide drugs for personalized therapy to light harvesting and electron conductive media for solar energy production and bioelectronics, respectively. In this study, we will discuss the self-assembly of selected model and bioactive peptides, in particular reviewing our recent work on the formation of peptide architectures of nano- and mesoscopic size in solution and on solid substrates. The hierarchical and cooperative characters of peptide self-assembly will be highlighted, focusing on the structural and dynamical properties of the peptide building blocks and on the nature of the intermolecular interactions driving the aggregation phenomena in a given environment. These results will pave the way for the understanding of the still-debated mechanism of action of an antimicrobial peptide (trichogin GA IV) and the pharmacokinetic properties of a pe...
Current Opinion in Biotechnology, 2019
One approach to designing de novo proteinaceous assemblies and materials is to develop simple, standardised building blocks and then to combine these symmetrically to construct more-complex higher-order structures. This has been done extensively using -structured peptides to produce peptide fibres and hydrogels. Here we focus on building with de novo helical peptides. Because of their self-contained, well-defined structures and clear sequence-to-structure relationships, helices are highly programmable making them robust building blocks for biomolecular construction. The progress made with this approach over the past two decades is astonishing and has led to a variety of de novo assemblies, including discrete nanoscale objects, and fibrous, nanotube, sheet and colloidal materials. This body of work provides an exceptionally strong foundation for advancing the field beyond in vitro design and into in vivo applications including what we call protein design in cells.
Langmuir, 2007
Inspired by recent work describing surfactant-like peptides, we have carried out a systematic study on peptides with the underlying composition of V 6 D 2 , altering the absolute sequence to determine the importance of the surfactant-like structure. All of the peptides examined here formed self-assembled structures in water. However, in contrast to other reports, we have found a surprising diversity of structures including fibers, tapes, and twisted ribbons but an absence of the vesicles and nanotubes described previously. Further investigations demonstrated that peptide purity plays a significant role in the outcome of the self-assembly. Different batches behave very differently, which can be linked to the compositions of these batches. This work shows that there is a need for not only rational design but also ease of synthesis of the building blocks for self-assembled structures.
International Journal of Molecular Sciences, 2015
Fabrication of self-assembled nanostructures is one of the important aspects in nanoscience and nanotechnology. The study of self-assembled soft materials remains an area of interest due to their potential applications in biomedicine. The versatile properties of soft materials can be tuned using a bottom up approach of small molecules. Peptide based self-assembly has significant impact in biology because of its unique features such as biocompatibility, straight peptide chain and the presence of different side chain functionality. These unique features explore peptides in various self-assembly process. In this review, we briefly introduce chemical reaction-mediated peptide self-assembly. Herein, we have emphasised enzymes, native chemical ligation and photochemical reactions in the exploration of peptide self-assembly.
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