Self-assembled arrays of peptide nanotubes by vapour deposition

Adler‐Abramovich, Lihi; Aronov, D. A.; Beker, P.; Yevnin, Maya; Stempler, Shiri; Buzhansky, Ludmila; Rosenman, G.; Gazit, Ehud

doi:10.1038/nnano.2009.298

Cited by 397 publications

(388 citation statements)

References 29 publications

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“…Novel approaches based on the dynamic self-assembly of inorganic building blocks [13][14][15] , actin self-organization 16 and the combination of top-down processes with peptide self-assembly have been reported recently 17 . In particular, Stupp and co-workers have described a self-assembling membrane system obtained through strong electrostatic interactions between PAs and oppositely charged polysaccharides 18 .…”

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confidence: 99%

Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein–peptide system

et al. 2015

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ature uses self-assembly to create a widespread variety of complex structures with elaborate geometries and outstanding properties 1 such as hierarchical order, adaptability, selfhealing and bioactivity. Developing new bioinspired processes based on dynamic self-assembly could facilitate the fabrication of synthetic three-dimensional (3D) materials with enhanced complexity, dynamic properties and functionality 2 . Proteins are particularly attractive building blocks because of their versatility and biofunctionality 3 . Elastin-like polypeptides (ELPs) 4 are recombinant proteins that have generated great interest 5 as a result of their modular structure, bioactivity, ease of design and production, and the possibility to create robust and elastic materials 5,6 . ELPs allow for a tunable molecular design 7 and are based on the tropoelastin recurrent motif Val-Pro-Gly-X-Gly (VPGXG), in which X is any amino acid other than proline 7 . This repeating pentapeptide provides ELPs with a thermoresponsive behaviour. Below a critical transition temperature (T t ), the ELP molecule undergoes a reversible-phase transition wherein the protein is soluble in aqueous solution and becomes highly solvated, surrounded by clatharate-like water structures. Above the T t , the hydrophobic domains dehydrate and the protein chain hydrophobically collapses and aggregates to form a phaseseparated state 8 .The use of natural and synthetic proteins to create functional materials has been hindered by the difficulty in controlling their conformation and nanoscale assembly with the precision required to form macroscopic materials. This limitation has driven the development of simpler and more-predictable peptide-based materials 9,10 . Peptide amphiphiles (PAs), for example, are synthetic molecules that can self-assemble into nanofibres and create functional 3D hydrogels that emulate the fibrous architecture of the extracellular matrix (ECM) 11,12 . Nonetheless, most peptide and/or protein materials are formed through equilibrium-based self-assembly approaches that are capable of generating stable supramolecular structures, but with limited hierarchy and spatiotemporal control, which has hindered their functionality 2 .Novel approaches based on the dynamic self-assembly of inorganic building blocks [13][14][15] , actin self-organization 16 and the combination of top-down processes with peptide self-assembly have been reported recently 17 . In particular, Stupp and co-workers have described a self-assembling membrane system obtained through strong electrostatic interactions between PAs and oppositely charged polysaccharides 18 . However, the possibility to exploit the unique structural and functional properties of proteins to create dynamic hierarchical materials remains an elusive target. In this study, we attempt to overcome this hurdle by using self-assembling peptides to promote protein conformational changes and guide their assembly into complex, yet functional, materials. We report the discovery and development of a protein/peptide system t...

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Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein–peptide system

et al. 2015

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“…Thus, self-assembling peptides can be employed as promising nanomaterials for the construction of ultracapacitors to store energy. 131 In future, it is conceivable that on the basis of this technology large-scale arrays of arranged peptide nanotubes or nanowires will be fabricated which then can be utilized as high-surface-area electrodes for energy storage applications, for microfluidic devices and for smart surfaces with favourable selfcleaning abilities due to their highly hydrophobic properties. Several other groups have investigated FF nanotubes for different nanofabrication purposes exploiting their strong stiffness and their stability under defined conditions, as for example Castillo-León, Svendsen and colleagues.…”

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Amyloid-based nanosensors and nanodevices

2014

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Self-assembling amyloid-like peptides and proteins give rise to promising biomaterials with potential applications in many fields. Amyloid structures are formed by the process of molecular recognition and self-assembly, wherein a peptide or protein monomer spontaneously self-associates into dimers and oligomers and subsequently into supramolecular aggregates, finally resulting in condensed fibrils. Mature amyloid fibrils possess a quasi-crystalline structure featuring a characteristic fiber diffraction pattern and have well-defined properties, in contrast to many amorphous protein aggregates that arise when proteins misfold. Core sequences of four to seven amino acids have been identified within natural amyloid proteins. They are capable to form amyloid fibers and fibrils and have been used as amyloid model structures, simplifying the investigations on amyloid structures due to their small size. Recent studies have highlighted the use of self-assembled amyloid-based fibers as nanomaterials. Here, we discuss the latest advances and the major challenges in developing amyloids for future applications in nanotechnology and nanomedicine, with the focus on development of sensors to study protein-ligand interactions.

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“…It has been recognized as the core recognition motif to drive selfassembly in Alzheimer's disease. Many studies have been carried out to self-assemble FF dipeptides into different nanostructures including nanoparticles, nanotubes, nanovesicles, and nanowires, shown in Figure 2 [34,[38][39][40][41][42]. FF selfassembled nanotubes have been demonstrated to be thermally stable, which is one of the most unique properties for bioinspired materials [43].…”

Section: Dipeptidementioning

confidence: 99%

“…FF selfassembled nanotubes have been demonstrated to be thermally stable, which is one of the most unique properties for bioinspired materials [43]. The high yield of FF dipeptides self-assembled nanotubes was achieved through vapor deposition method, which could tune the density and length of nanotubes by controlling the monomer supply [38]. FF selfassembled nanotubes were also obtained through dissolving the dipeptides in water by sonication followed by heating.…”

Section: Dipeptidementioning

confidence: 99%

Peptide Self-Assembled Nanostructures for Drug Delivery Applications

Fan

Shen

et al. 2017

Journal of Nanomaterials

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Peptide self-assembled nanostructures are very popular in many biomedical applications. Drug delivery is one of the most promising applications among them. The tremendous advantages for peptide self-assembled nanostructures include good biocompatibility, low cost, tunable bioactivity, high drug loading capacities, chemical diversity, specific targeting, and stimuli responsive drug delivery at disease sites. Peptide self-assembled nanostructures such as nanoparticles, nanotubes, nanofibers, and hydrogels have been investigated by many researchers for drug delivery applications. In this review, the underlying mechanisms for the self-assembled nanostructures based on peptides with different types and structures are introduced and discussed. Peptide self-assembled nanostructures associated promising drug delivery applications such as anticancer drug and gene drug delivery are highlighted. Furthermore, peptide self-assembled nanostructures for targeted and stimuli responsive drug delivery applications are also reviewed and discussed.

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Self-assembled arrays of peptide nanotubes by vapour deposition

Cited by 397 publications

References 29 publications

Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein–peptide system

Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein–peptide system

Amyloid-based nanosensors and nanodevices

Peptide Self-Assembled Nanostructures for Drug Delivery Applications

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