Self-Assembly of Large and Small Molecules into Hierarchically Ordered Sacs and Membranes

Capito, Ramille M.; Azevedo, Helena S.; Velichko, Yuri S.; Mata, Álvaro; Stupp, Samuel I.

doi:10.1126/science.1154586

Cited by 586 publications

(595 citation statements)

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“…3a) and weaker membranes as observed on manipulation. Interestingly, no membranes with the multilayered architecture were formed when using PAK2 (that is, ELP2/PAK2, ELP4/PAK2 and ELP5/PAK2), but rather were structurally similar to the PA/polysaccharide system reported by Stupp and co-workers 18,27 , as observed by SEM (Fig. 3a) and SAXS (Fig.…”

Section: Resultssupporting

confidence: 49%

“…In this way, a closed membrane is formed that entraps the PA solution inside it and leaves the ELP solution outside. Self-assembled membranes formed at the interface between a solution of linear polyelectrolytes and a solution of either oppositely charged PAs [18][19][20][21][22] or surfactant molecules 23 have been reported. However, in our system, within the first minute of formation and on contact with any surface, the membrane spontaneously, yet controllably, adheres, focally opens and seals to the surface (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Strong electrostatic forces have been shown to drive the assembly of interfacial systems 18,22,23 . Zeta potential (ζ) measurements demonstrated that the ELP5 and PAK3 need to be oppositely charged to co-assemble into the dynamic system (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The fifth block contains an Arg-Gly-Asp-Ser (RGDS) motif to promote cell adhesion. The PAK3 (Table 2) is a nine amino acid peptide attached to an alkyl tail of 16 carbons capable of self-assembling into nanofibres when the charges of its peptide segment are screened 18,19 . It was found positively charged below its isoelectric point of 10.3 (Table 2 and Supplementary Fig.…”

Section: Resultsmentioning

confidence: 99%

“…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.…”

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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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Section: Resultssupporting

confidence: 49%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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

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Peptide Self‐Assembly

Cavalli

Marsden

Alberício

et al. 2012

Supramolecular Chemistry

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The formation of well‐ordered nanostructures by a process of self‐association in aqueous media or at interfaces represents the core of modern nanotechnology. Processes of molecular recognition and self‐assembly direct the way in which relatively simple building blocks recognize each other, associate, and form ordered one‐, two‐, and three‐dimensional structures with a wide range of applications in nanoscience. The manner in which molecules self‐assemble and their interaction energies, shapes, and ultimate functions can be programmed at the molecular level by a careful and rational design. Peptides are among the most powerful building blocks available for constructing “smart” well‐ordered nanostructures in a “bottom‐up” approach, as they possess the biocompatibility and chemical diversity that are commonly found in proteins, but they are much more stable and robust and can be readily synthesized on a large scale. In this chapter, the main categories of peptide amphiphiles are discussed for their ability to spontaneously associate to form a variety of nanostructures (e.g., tubes, spheres, fibrils, tapes, and hydrogels at the nanometerscale) and some key features of this processes are outlined by describing a selection of relevant published works.

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Self‐Assembly Systems

Lee

2011

Self‐Assembly and Nanotechnology Systems

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Self-Assembly of Large and Small Molecules into Hierarchically Ordered Sacs and Membranes

Cited by 586 publications

References 18 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

Peptide Self‐Assembly

Self‐Assembly Systems

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