Protein nanoparticles as multifunctional biocatalysts and health assessment sensors

Raeeszadeh‐Sarmazdeh, Maryam; Hartzell, Emily J; Price, J. M.; Chen, Wilfred

doi:10.1016/j.coche.2016.08.016

Cited by 26 publications

(26 citation statements)

References 64 publications

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“…Growing interest in the use of protein nanoparticles for applications in medicine and materials science has stimulated efforts to design new protein cages from a range of protein building blocks . Our efforts have focused on the use of de novo ‐designed coiled coils as “off‐the‐shelf” components to assemble proteins into cages .…”

Section: Discussionmentioning

confidence: 99%

“…Examples include actin and tubulin fibers, viral capsids, pyruvate dehydrogenase complex (PDH), ferritin, and the bacterial carboxysome . The ability of proteins to assemble into such diverse higher‐order architectures has made them attractive systems for designing biological nano‐materials with applications in medicine, synthetic biology, and materials science …”

Section: Introductionmentioning

confidence: 99%

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Elaborating a coiled‐coil‐assembled octahedral protein cage with additional protein domains

et al. 2018

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De novo design of protein nano-cages has potential applications in medicine, synthetic biology, and materials science. We recently developed a modular, symmetry-based strategy for protein assembly in which short, coiled-coil sequences mediate the assembly of a protein building block into a cage. The geometry of the cage is specified by the combination of rotational symmetries associated with the coiled-coil and protein building block. We have used this approach to design well-defined octahedral and tetrahedral cages. Here, we show that the cages can be further elaborated and functionalized by the addition of another protein domain to the free end of the coiled-coil: in this case by fusing maltose-binding protein to an octahedral protein cage to produce a structure with a designed molecular weight of ~1.8 MDa. Importantly, the addition of the maltose binding protein domain dramatically improved the efficiency of assembly, resulting in ~ 60-fold greater yield of purified protein compared to the original cage design. This study shows the potential of using small, coiled-coil motifs as off-the-shelf components to design MDa-sized protein cages to which additional structural or functional elements can be added in a modular manner.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Elaborating a coiled‐coil‐assembled octahedral protein cage with additional protein domains

et al. 2018

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“…Virus particles such as tobacco mosaic virus (TMV), cowpea mosaic virus (CPMV), cowpea chlorotic mottle virus (CCMV) or the bacteriophage M13 are frequently used biotemplates for efficient analyte detection in sensing devices (as e.g. reviewed in 26 - 29 ). These particles offer well-defined, nanostructured and stable protein backbones enabling the multivalent presentation of functional groups.…”

Section: Introductionmentioning

confidence: 99%

Penicillin Detection by Tobacco Mosaic Virus-Assisted Colorimetric Biosensors

Koch¹,

Poghossian²,

Schöning³

et al. 2018

Nanotheranostics

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The presentation of enzymes on viral scaffolds has beneficial effects such as an increased enzyme loading and a prolonged reusability in comparison to conventional immobilization platforms. Here, we used modified tobacco mosaic virus (TMV) nanorods as enzyme carriers in penicillin G detection for the first time. Penicillinase enzymes were conjugated with streptavidin and coupled to TMV rods by use of a bifunctional biotin-linker. Penicillinase-decorated TMV particles were characterized extensively in halochromic dye-based biosensing. Acidometric analyte detection was performed with bromcresol purple as pH indicator and spectrophotometry. The TMV-assisted sensors exhibited increased enzyme loading and strongly improved reusability, and higher analysis rates compared to layouts without viral adapters. They extended the half-life of the sensors from 4 - 6 days to 5 weeks and thus allowed an at least 8-fold longer use of the sensors. Using a commercial budget-priced penicillinase preparation, a detection limit of 100 µM penicillin was obtained. Initial experiments also indicate that the system may be transferred to label-free detection layouts.

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“…These spherical nanostructures are highly attractive owing to their particle uniformity, biocompatibility, and precise controllability. Being able to fine-tune the morphological architecture and functions of these particulate scaffolds has made them excellent candidates for the design of biocatalytic nanoreactors (Raeeszadeh-Sarmazdeh et al, 2016;Lee, 2018;Schmid-Dannert and López-Gallego, 2019). EZPs can be reprogrammed to incorporate various foreign biological functions such as, e.g., enzymes of industrial interest.…”

Section: Enzyme-derived Nanoparticles (Ezps)mentioning

confidence: 99%

“…Several promising biological supramolecular assemblies, such as polyhydroxyalkanoate (PHA) particles Parlane et al, 2016b), virus-like particles (VLPs) (Schwarz et al, 2017;Wilkerson et al, 2018), enzyme-derived nanoparticles (EZPs) (Raeeszadeh-Sarmazdeh et al, 2016;Diaz et al, 2018;Schmid-Dannert and López-Gallego, 2019), membrane vesicles Sharma et al, 2018), and magnetosomes (Jacob and Suthindhiran, 2016;Yan et al, 2017) have been studied to immobilize a variety of functional proteins, including industrially relevant enzymes using recombinant fusion technology (Figure 1). Briefly, genetically amenable components of these scaffolds are translationally fused with proteins of interest, such as, e.g., enzymes, and are produced in a range of recombinant expression systems, like various prokaryotic and eukaryotic organisms.…”

mentioning

confidence: 99%

Bioengineered Polyhydroxyalkanoates as Immobilized Enzyme Scaffolds for Industrial Applications

Wong

Ogura

Chen

et al. 2020

Front. Bioeng. Biotechnol.

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Enzymes function as biocatalysts and are extensively exploited in industrial applications. Immobilization of enzymes using support materials has been shown to improve enzyme properties, including stability and functionality in extreme conditions and recyclability in biocatalytic processing. This review focuses on the recent advances utilizing the design space of in vivo self-assembled polyhydroxyalkanoate (PHA) particles as biocatalyst immobilization scaffolds. Self-assembly of biologically active enzyme-coated PHA particles is a one-step in vivo production process, which avoids the costly and laborious in vitro chemical cross-linking of purified enzymes to separately produced support materials. The homogeneous orientation of enzymes densely coating PHA particles enhances the accessibility of catalytic sites, improving enzyme function. The PHA particle technology has been developed into a remarkable scaffolding platform for the design of cost-effective designer biocatalysts amenable toward robust industrial bioprocessing. In this review, the PHA particle technology will be compared to other biological supramolecular assembly-based technologies suitable for in vivo enzyme immobilization. Recent progress in the fabrication of biological particulate scaffolds using enzymes of industrial interest will be summarized. Additionally, we outline innovative approaches to overcome limitations of in vivo assembled PHA particles to enable finetuned immobilization of multiple enzymes to enhance performance in multi-step cascade reactions, such as those used in continuous flow bioprocessing.

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Protein nanoparticles as multifunctional biocatalysts and health assessment sensors

Cited by 26 publications

References 64 publications

Elaborating a coiled‐coil‐assembled octahedral protein cage with additional protein domains

Elaborating a coiled‐coil‐assembled octahedral protein cage with additional protein domains

Penicillin Detection by Tobacco Mosaic Virus-Assisted Colorimetric Biosensors

Bioengineered Polyhydroxyalkanoates as Immobilized Enzyme Scaffolds for Industrial Applications

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