Modular genetic design of multi-domain functional amyloids: insights into self-assembly and functional properties

Cui, Mengkui; Qi, Qi; Gurry, Thomas; Zhao, Tianxin; An, Bo; Pu, Jiahua; Gui, Xingmin; Cheng, Allen A.; Zhang, Siyu; Xun, Dongmin; Becce, Michele; Briatico‐Vangosa, Francesco; Liu, Cong; Lu, Timothy K.; Zhong, Chao

doi:10.1039/c9sc00208a

Cited by 20 publications

(29 citation statements)

References 54 publications

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“…To mimic the multiscale mineralization of diatom frustules, we started by rationally designing self-assembling nanofiber networks capable of both promoting local silica nucleation and mineralization at the molecular level and recapturing protein–polysaccharide interactions that occur in diatom frustules. Specifically, we initially constructed and tested mineralization-promoting CsgA fusion proteins by genetically appending a SiO 2 -nucleation peptide (R5) at the N-terminus of CsgA ( R5 CsgA), a bacterial structural amyloid protein of E. coli biofilms that is amenable for genetic modification to endow functional properties without disrupting its nanofiber self-assembly capability [ 37 , 43 ]. We confirmed that the R5 CsgA fusion proteins could self-assemble into amyloid nanofibers ( Supplementary Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Further, structural characterization by X-ray fiber diffraction revealed that the nanofibers displayed a typical β diffraction pattern, with a meridional reflection (denoted as d 2 in the diffraction pattern) at 4.8 Å, reflecting the spacing between β-strands within each layer of β-sheets and an equatorial reflection (denoted as d 1 in the diffraction patterns) at 9.5 Å, corresponding to inter-sheet packing distances (Fig. 2C ) [ 43 ].…”

Section: Resultsmentioning

confidence: 99%

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Diatom-inspired multiscale mineralization of patterned protein–polysaccharide complex structures

Wang

et al. 2020

National Science Review

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Marine diatoms construct their hierarchically ordered, three-dimensional (3D) external structures called frustules through precise biomineralization processes. Recapitulating the remarkable architectures and functions of diatom frustules in artificial materials is a major challenge that has important technological implications for hierarchically ordered composites. Here, we report the construction of highly ordered, mineralized composites based on fabrication of complex self-supporting porous structures—made of genetically engineered amyloid fusion proteins and the natural polysaccharide chitin—and performing in situ multiscale protein-mediated mineralization with diverse inorganic materials, including SiO2, TiO2, and Ga2O3. Subsequently, using sugar cubes as templates, we demonstrate that 3D fabricated porous structures can become colonized by engineered bacteria and can be functionalized with highly photoreactive minerals, thereby enabling co-localization of the photocatalytic units with a bacteria-based hydrogenase reaction for a successful semi-solid artificial photosynthesis system for hydrogen evolution. Our study thus highlights the power of coupling genetically engineered proteins and polysaccharides with biofabrication techniques to generate hierarchically organized mineralized porous structures inspired by nature.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Diatom-inspired multiscale mineralization of patterned protein–polysaccharide complex structures

Wang

et al. 2020

National Science Review

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“…The coating materials exhibit a typical cross-β diffraction pattern, which is the signature of amyloid fiber (Fig. 2A, top right) ( 32 , 33 ). Moreover, the x-ray fiber diffraction pattern of TLC-M nanofibers is close to that of TDP43 LC nanofibers (fig.…”

Section: Resultsmentioning

confidence: 99%

Exploiting mammalian low-complexity domains for liquid-liquid phase separation–driven underwater adhesive coatings

Cui

Wang

et al. 2019

Sci. Adv.

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Many biological materials form via liquid-liquid phase separation (LLPS), followed by maturation into a solid-like state. Here, using a biologically inspired assembly mechanism designed to recapitulate these sequential assemblies, we develop ultrastrong underwater adhesives made from engineered proteins containing mammalian low-complexity (LC) domains. We show that LC domain–mediated LLPS and maturation substantially promotes the wetting, adsorption, priming, and formation of dense, uniform amyloid nanofiber coatings on diverse surfaces (e.g., Teflon), and even penetrating difficult-to-access locations such as the interiors of microfluidic devices. Notably, these coatings can be deposited on substrates over a broad range of pH values (3 to 11) and salt concentrations (up to 1 M NaCl) and exhibit strong underwater adhesion performance. Beyond demonstrating the utility of mammalian LC domains for driving LLPS in soft materials applications, our study illustrates a powerful example of how combining LLPS with subsequent maturation steps can be harnessed for engineering protein-based materials.

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“…To date, the mechanisms behind the non-toxicity properties of functional amyloids are still unclear. However, Jackson and Hewitt suggested realistic ways to resolve this: (1) regulating the content of amyloidogenic peptides/proteins; (2) decreasing the time of the oligomers state during amyloidogenesis; (3) locating amyloids within membrane-bound organelles (e.g., melanosoma); and (4) regulating amyloid formation by other molecules and disassembling the fibrils under physiological conditions [ 229 ].…”

Section: Useful Properties Of Amyloids Functional Amyloidsmentioning

confidence: 99%

Amyloids: The History of Toxicity and Functionality

Yakupova

Bobyleva

Shumeyko

et al. 2021

Biology

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Proteins can perform their specific function due to their molecular structure. Partial or complete unfolding of the polypeptide chain may lead to the misfolding and aggregation of proteins in turn, resulting in the formation of different structures such as amyloid aggregates. Amyloids are rigid protein aggregates with the cross-β structure, resistant to most solvents and proteases. Because of their resistance to proteolysis, amyloid aggregates formed in the organism accumulate in tissues, promoting the development of various diseases called amyloidosis, for instance Alzheimer’s diseases (AD). According to the main hypothesis, it is considered that the cause of AD is the formation and accumulation of amyloid plaques of Aβ. That is why Aβ-amyloid is the most studied representative of amyloids. Therefore, in this review, special attention is paid to the history of Aβ-amyloid toxicity. We note the main problems with anti-amyloid therapy and write about new views on amyloids that can play positive roles in the different organisms including humans.

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Modular genetic design of multi-domain functional amyloids: insights into self-assembly and functional properties

Abstract: Modular genetic design of functional amyloids represents new opportunities for creating multifunctional molecular materials with tailored structures and performance.

Cited by 20 publications

References 54 publications

Diatom-inspired multiscale mineralization of patterned protein–polysaccharide complex structures

Diatom-inspired multiscale mineralization of patterned protein–polysaccharide complex structures

Exploiting mammalian low-complexity domains for liquid-liquid phase separation–driven underwater adhesive coatings

Amyloids: The History of Toxicity and Functionality

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