A self-assembly pathway to aligned monodomain gels

Zhang, Shuming; Greenfield, Megan; Mata, Álvaro; Palmer, Liam C.; Bitton, Ronit; Mantei, Jason R.; Aparicio, Conrado; Cruz, Mónica Olvera de la; Stupp, Samuel I.

doi:10.1038/nmat2778

Cited by 588 publications

(625 citation statements)

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“…Their data suggested that the local packing was not changed by heating and cooling, but that the aggregates were dehydrated by heating, leading to filaments with significantly greater diameters. This increase in diameter was backed up by changes in the SAXS data 16. Hence, our systems are behaving differently.…”

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confidence: 84%

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Opening a Can of Worm(‐like Micelle)s: The Effect of Temperature of Solutions of Functionalized Dipeptides

Draper

Brasnett

et al. 2017

Angew Chem Int Ed

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confidence: 84%

“…with respect to peptide amphiphiles,16 where heating and cooling led to a change in the properties of the solution and greater alignment of structures. The heating and cooling was found to be necessary to allow “noodling”, for example.…”

mentioning

confidence: 99%

Opening a Can of Worm(‐like Micelle)s: The Effect of Temperature of Solutions of Functionalized Dipeptides

Draper

Brasnett

et al. 2017

Angew Chem Int Ed

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“…For example, the solution viscosity increased significantly. 93 The gel that was formed on addition of a calcium salt was also significantly stiffer than when the salt was added to a solution that had not been heated and cooled before the addition of the salt. The increased viscosity also allowed ''noodles'' to be drawn out.…”

Section: Process Of Assemblymentioning

confidence: 99%

Low-Molecular-Weight Gels: The State of the Art

Draper

Adams

2017

Chem

536

469

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Low-molecular-weight gels are currently a hugely important class of materials that are attracting significant interest. These gels are formed when small molecules self-assemble into one-dimensional structures that entangle and cross-link to form a network that is capable of immobilizing the solvent. Here, we critically discuss the current state of the art and highlight two key areas where we believe there is significant untapped potential. The first is the observation that the properties of the gels are highly process dependent, which means that it is possible to access materials with very different properties from a single gelator. Second, using multiple gelators offers the opportunity to prepare materials with a high degree of information content and with a wider range of properties. We aim to spark thought and discussion on these aspects. INTRODUCTIONLow-molecular-weight gels (LMWGs), or supramolecular gels, are a fascinating and useful class of material. The gels arise from the self-assembly of small molecules into long, anisotropic structures, most commonly fibers. [1][2][3][4][5] At a sufficiently high concentration, these fibers entangle or otherwise form cross-links, leading to the network that is able to immobilize the solvent through surface tension and capillary forces. 1,2 These gels differ from permanently covalently cross-linked polymer gels because the cross-linking can be reversed by the input of energy, for example, by heating. 6 LMWGs have been around for many years but are receiving considerable current interest. 4 They are also used in industrial products, 7 although this seems rarely discussed in the academic literature.In addition to the industrial applications, many recent advances and uses are being described. [8][9][10][11][12] The specific self-assembly leading to gel formation can be exploited. For example, the fiber formation is a result of molecular stacking, meaning that the self-assembly leads to aggregates that can be suitable for optoelectronic applications. 13,14 The ready reversibility of gelation can be exploited, for example, to release cells from gels on demand in a manner that does not lead to cell death. 15 Ready gel formation by a simple trigger can also be used to allow easy and efficient gel loading. [16][17][18] Unsurprisingly, therefore, there is significant interest in these materials ( Figure 1). This is a fascinating area and in many ways holds attention because of the difficulties in probing and understanding the gels. The gels arise from assembly across many length scales, and understanding all of these is difficult. At the molecular level, the molecules must interact in a manner that leads to the formation of suitable aggregates that can eventually entangle. Thus, one-dimensional growth must be favored. From this perspective, it is very frustrating that it is often extremely difficult to predict whether a molecule will form a gel or not; indeed, gelation has been described as an empirical science. 4 Structurally similar small molecules can exhibitThe Bigger Pict...

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“…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 .…”

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

et al. 2015

Self Cite

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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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A self-assembly pathway to aligned monodomain gels

Cited by 588 publications

References 34 publications

Opening a Can of Worm(‐like Micelle)s: The Effect of Temperature of Solutions of Functionalized Dipeptides

Opening a Can of Worm(‐like Micelle)s: The Effect of Temperature of Solutions of Functionalized Dipeptides

Low-Molecular-Weight Gels: The State of the Art

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

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