Self‐Assembly in Protein‐Based Bionanomaterials

Solomonov, Alexey V.; Shimanovich, Ulyana

doi:10.1002/ijch.201900083

Cited by 32 publications

(18 citation statements)

References 258 publications

(398 reference statements)

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“…Natural silks are produced by many insects and arthropods 4,5 . Notably, spider silk and silkworm silk have been the subject of much interest due to the former's incredible toughness and the latter's potential for genetic modification and commercial production [6][7][8][9][10] .…”

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confidence: 99%

Micro and nano-scale compartments guide the structural transition of silk protein monomers into silk fibers

et al. 2022

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Silk is a unique, remarkably strong biomaterial made of simple protein building blocks. To date, no synthetic method has come close to reproducing the properties of natural silk, due to the complexity and insufficient understanding of the mechanism of the silk fiber formation. Here, we use a combination of bulk analytical techniques and nanoscale analytical methods, including nano-infrared spectroscopy coupled with atomic force microscopy, to probe the structural characteristics directly, transitions, and evolution of the associated mechanical properties of silk protein species corresponding to the supramolecular phase states inside the silkworm’s silk gland. We found that the key step in silk-fiber production is the formation of nanoscale compartments that guide the structural transition of proteins from their native fold into crystalline β-sheets. Remarkably, this process is reversible. Such reversibility enables the remodeling of the final mechanical characteristics of silk materials. These results open a new route for tailoring silk processing for a wide range of new material formats by controlling the structural transitions and self-assembly of the silk protein’s supramolecular phases.

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Micro and nano-scale compartments guide the structural transition of silk protein monomers into silk fibers

et al. 2022

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“…Examples of such systems include full-length versions of proteins such as fused in sarcoma (FUS), other proteins from the FET family, and disordered prion-like domains (PLDs) excised from these and other systems. ,− Condensates can undergo hardening behavior over time through non-equilibrium transitions such as dynamical arrest and physical aging. − Changes to material properties in condensates can also be realized through equilibrium solidification transitions and/or fibril formation, , wherein condensates serve as crucibles for driving equilibrium transitions. − Mutations within PLDs of FUS and related proteins are associated with the formation of protein-rich deposits in the context of amyotrophic lateral sclerosis (ALS). ,,, McKnight and co-workers showed that archetypal PLDs from FUS and related proteins can form self-supporting hydrogels characterized by physically cross-linked fibrils. − , Structural studies using peptide-based microcrystals led Hughes et al to propose that specific motifs known as low-complexity, aromatic-rich, kinked segments or LARKS provide the cohesive interactions to drive the formation of networks that scaffold peptide or protein-based hydrogels . These hydrogels are biochemical facsimiles of self-assembled fibrillar networks or SAFINS that are formed by synthetic associative polymers and proteins/peptides with or without low-molecular weight organic gelators. − It is noteworthy that hydrogels and fibrils form above concentrations that are in the high micromolar to millimolar range. Patel et al, as well as Molliex et al, showed that systems such as the PLDs of FUS and hnRNPA1 and full-length hnRNPA1 can also undergo phase separation and percolation or the less nuanced liquid–liquid phase separation (LLPS) to form spherical, fluid-like condensates at bulk concentrations that are at least 1–2 orders of magnitude lower than the threshold concentrations for fibril formation.…”

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Glycine-Rich Peptides from FUS Have an Intrinsic Ability to Self-Assemble into Fibers and Networked Fibrils

et al. 2021

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Glycine-rich regions feature prominently in intrinsically disordered regions (IDRs) of proteins that drive phase separation and the regulated formation of membraneless biomolecular condensates. Interestingly, the Gly-rich IDRs seldom feature poly-Gly tracts. The protein fused in sarcoma (FUS) is an exception. This protein includes two 10-residue poly-Gly tracts within the prion-like domain (PLD) and at the interface between the PLD and the RNA binding domain. Poly-Gly tracts are known to be highly insoluble, being potent drivers of self-assembly into solid-like fibrils. Given that the internal concentrations of FUS and FUS-like molecules cross the high micromolar and even millimolar range within condensates, we reasoned that the intrinsic insolubility of poly-Gly tracts might be germane to emergent fluid-to-solid transitions within condensates. To assess this possibility, we characterized the concentration-dependent self-assembly for three non-overlapping 25-residue Gly-rich peptides derived from FUS. Two of the three peptides feature 10-residue poly-Gly tracts. These peptides form either long fibrils based on twisted ribbon-like structures or self-supporting gels based on physical cross-links of fibrils. Conversely, the peptide with similar Gly contents but lacking a poly-Gly tract does not form fibrils or gels. Instead, it remains soluble across a wide range of concentrations. Our findings highlight the ability of poly-Gly tracts within IDRs that drive phase separation to undergo self-assembly. We propose that these tracts are likely to contribute to nucleation of fibrillar solids within dense condensates formed by FUS.

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“…Excellent reviews have covered the topic of protein self-assembly and highlighted its broad reach across protein design and engineering, chemical and structural biology, bio- and nanotechnology, and materials science. ,− Our primary goal is not only to update those reviews with the most recent examples from the literature but also to provide a logical framework that we believe aptly describes the progression of the field from structure-building to property- and function-building. Although we acknowledge the key importance of disordered or heterogeneous protein ensembles, our focus here will be entirely on the design and construction of structurally well-defined, compositionally uniform protein assemblies, which lend themselves more readily to establishing design–structure–property–function relationships.…”

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confidence: 99%

Protein Assembly by Design

et al. 2021

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Proteins are nature’s primary building blocks for the construction of sophisticated molecular machines and dynamic materials, ranging from protein complexes such as photosystem II and nitrogenase that drive biogeochemical cycles to cytoskeletal assemblies and muscle fibers for motion. Such natural systems have inspired extensive efforts in the rational design of artificial protein assemblies in the last two decades. As molecular building blocks, proteins are highly complex, in terms of both their three-dimensional structures and chemical compositions. To enable control over the self-assembly of such complex molecules, scientists have devised many creative strategies by combining tools and principles of experimental and computational biophysics, supramolecular chemistry, inorganic chemistry, materials science, and polymer chemistry, among others. Owing to these innovative strategies, what started as a purely structure-building exercise two decades ago has, in short order, led to artificial protein assemblies with unprecedented structures and functions and protein-based materials with unusual properties. Our goal in this review is to give an overview of this exciting and highly interdisciplinary area of research, first outlining the design strategies and tools that have been devised for controlling protein self-assembly, then describing the diverse structures of artificial protein assemblies, and finally highlighting the emergent properties and functions of these assemblies.

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Self‐Assembly in Protein‐Based Bionanomaterials

Cited by 32 publications

References 258 publications

Micro and nano-scale compartments guide the structural transition of silk protein monomers into silk fibers

Micro and nano-scale compartments guide the structural transition of silk protein monomers into silk fibers

Glycine-Rich Peptides from FUS Have an Intrinsic Ability to Self-Assemble into Fibers and Networked Fibrils

Protein Assembly by Design

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