Pursuing the Promise of Enzymatic Enhancement with Nanoparticle Assemblies

Vranish, James N.; Ancona, Mario G.; Walper, Scott A.; Medintz, Igor L.

doi:10.1021/acs.langmuir.7b02588

Cited by 51 publications

(90 citation statements)

References 146 publications

(334 reference statements)

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“…Note that this is relative to the efficiency of each PTE. The authors note that this is consistent with other reports where the most enhancement was seen with low enzyme:NP ratios [19,22,39,81,82]. Why is there a "sweet-spot" at all in regards to NP size?…”

Section: Factors Affecting Immobilization Benefits-scaffold Size Scasupporting

confidence: 89%

“…Enzymes can be immobilized either as single copies or as multiple enzymes which are part of a multienzyme cascade [4,[17][18][19][20][21][22]. Benefits of immobilizing single enzymes can include: (1) increased stability, (2) increased activity, (3) closeness and orientation to substrate, and (4) increased recoverability and reuse; whereas, the benefits of immobilizing multiple enzymes can include these plus: (5) increased (temporary) reaction rates, (6) bypassed intermediate toxicity, (7) bypassed offtarget pathways/directed catalysis, (8) reaction order, and (9) modularity ( Figure 1, Table 1) [4,10,[23][24][25][26][27][28][29][30].…”

Section: Benefits Of Enzyme Immobilizationmentioning

confidence: 99%

“…Overall, enzyme immobilization can offer inherent benefits, and these can be particularly exploited when working at the nanoscale with NPs. Advantages of NPs include: (1) multiple mechanisms for enzyme attachment; (2) high surface area to volume ratios and corresponding high radii of curvature leading to relatively large distances between enzymes and limiting detrimental protein-protein interactions; (3) the potential for multi-point attachment of (multi-subunit) enzymes, allowing in some cases increased enzyme stability; (4) the ability to structure solvent up to~2 × NP diameter, effecting many properties (e.g., pH gradients and boundary layers) that could affect substrate/intermediate/product partitioning; and (5) the ability to diffuse, whereas planar surfaces may have boundary layer and stagnation effects [19,22,42,[59][60][61][62][63][64]. While many NPs have been used for enzyme immobilization (silica, magnetic, silver, etc.…”

Section: Benefits Of Enzyme Immobilizationmentioning

confidence: 99%

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Quantum Dots and Gold Nanoparticles as Scaffolds for Enzymatic Enhancement: Recent Advances and the Influence of Nanoparticle Size

et al. 2020

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Nanoparticle scaffolds can impart multiple benefits onto immobilized enzymes including enhanced stability, activity, and recoverability. The magnitude of these benefits is modulated by features inherent to the scaffold–enzyme conjugate, amongst which the size of the nanoscaffold itself can be critically important. In this review, we highlight the benefits of enzyme immobilization on nanoparticles and the factors affecting these benefits using quantum dots and gold nanoparticles as representative materials due to their maturity. We then review recent literature on the use of these scaffolds for enzyme immobilization and as a means to dissect the underlying mechanisms. Detailed analysis of the literature suggests that there is a “sweet-spot” for scaffold size and the ratio of immobilized enzyme to scaffold, with smaller scaffolds and lower enzyme:scaffold ratios generally providing higher enzymatic activities. We anticipate that ongoing studies of enzyme immobilization onto nanoscale scaffolds will continue to sharpen our understanding of what gives rise to beneficial characteristics and allow for the next important step, namely, that of translation to large-scale processes that exploit these properties.

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Section: Factors Affecting Immobilization Benefits-scaffold Size Scasupporting

confidence: 89%

Section: Benefits Of Enzyme Immobilizationmentioning

confidence: 99%

Section: Benefits Of Enzyme Immobilizationmentioning

confidence: 99%

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Quantum Dots and Gold Nanoparticles as Scaffolds for Enzymatic Enhancement: Recent Advances and the Influence of Nanoparticle Size

et al. 2020

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“…Only the DHLA‐PEG600‐COOH ligand was observed to work well for both the trypsin and chymotrypsin upstream sensing assemblies to yield efficient QD‐Cy3 FRET as manifested in QD donor quenching and Cy3 sensitization. Although we do not currently understand the difference in observed properties of QD ligands versus PD, we suggest it is a consequence of the complex relationship among the ligand conformation, the buffer, the PD sequence, and the localized QD‐dye properties …”

Section: Resultsmentioning

confidence: 89%

Transducing Protease Activity into DNA Output for Developing Smart Bionanosensors

Bui

Brown

Buckhout‐White

et al. 2019

Small

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DNA can process information through sequence‐based reorganization but cannot typically receive input information from most biological processes and translate that into DNA compatible language. Coupling DNA to a substrate responsive to biological events can address this limitation. A two‐component sensor incorporating a chimeric peptide‐DNA substrate is evaluated here as a protease‐to‐DNA signal convertor which transduces protease activity through DNA gates that discriminate between different input proteases. Acceptor dye‐labeled peptide‐DNAs are assembled onto semiconductor quantum dot (QD) donors as the input gate. Addition of trypsin or chymotrypsin cleaves their cognate peptide sequence altering the efficiency of Förster resonance energy transfer (FRET) with the QD and frees a DNA output which interacts with a tetrahedral output gate. Downstream output gate rearrangement results in FRET sensitization of a new acceptor dye. Following characterization of component assembly and optimization of individual steps, sensor ability to discriminate between the two proteases is confirmed along with effects from joint interactions where potential for cross‐talk is highest. Processing multiple bits of information for a sensing outcome provides more confidence than relying on a single change especially for the discrimination between different targets. Coupling other substrates to DNA that respond similarly could help target other types of enzymes.

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“…The pursuing of efficient supports to improve enzyme performance has been one of the most important directions in biotechnology since the first example of enzyme immobilization in 1916 [1][2][3]. The rapid growth in nanotechnology offers a wealth of opportunities for the successful combination of enzymes with various nanostructured materials, namely enzyme-nanostructure biocatalysts (nanobiocatalysts) [4][5][6][7][8][9]. In contrast to conventional bulk supports, nanostructured supports possess plenty of advantages, such as large specific surface area, reduced mass transfer limitation, ease of surface modifications, unique geometry and size/shape-dependent characteristics.…”

Section: Introductionmentioning

confidence: 99%

Recent Advances in Enzyme-Nanostructure Biocatalysts with Enhanced Activity

Zhang

et al. 2020

Catalysts

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Owing to their unique physicochemical properties and comparable size to biomacromolecules, functional nanostructures have served as powerful supports to construct enzyme-nanostructure biocatalysts (nanobiocatalysts). Of particular importance, recent years have witnessed the development of novel nanobiocatalysts with remarkably increased enzyme activities. This review provides a comprehensive description of recent advances in the field of nanobiocatalysts, with systematic elaboration of the underlying mechanisms of activity enhancement, including metal ion activation, electron transfer, morphology effects, mass transfer limitations, and conformation changes. The nanobiocatalysts highlighted here are expected to provide an insight into enzyme-nanostructure interaction, and provide a guideline for future design of high-efficiency nanobiocatalysts in both fundamental research and practical applications.Catalysts 2020, 10, 338 2 of 15 nanoscale supports, such as nanoparticles, nanowires, microspheres, metal-organic frameworks, and nanoflowers, has also drawn extensive attention in recent years [5,[16][17][18][19][20][21][22]. A great deal of effort has also been made to design nanostructured supports with a variety of components including noble metal (e.g., Au) [23,24], metal oxides (e.g., Cu 2 O, Fe 3 O 4 , SiO 2 , Ti 8 O 15 , alumina) [16,25-33], polymer (e.g., Cu 2+ /PAA/PPEGA matrix, aldehyde-derived Pluronic polymer, polycaprolactone) [34-36], metal-organic frameworks (e.g., zeolitic imidazolate framework) [37-39], carbon based (e.g., carbon dots, carbon nanotubes) [40-44], and complex compounds (e.g., Cu 3 (PO 4 ) 2 ·3H 2 O, Ca 3 (PO 4 ) 2 , Co 3 (PO 4 ) 2 ·8H 2 O, Mn 3 (PO 4 ) 2 , Ca 8 H 2 (PO 4 ) 6 , Cu 4 (OH) 6 )SO 4 , CaHPO 4 , Zn 3 (PO 4 ) 2 , Mg-Al layered double hydroxide, CdSe/ZnS quantum dots) [17,[45][46][47][48][49][50][51][52][53][54][55][56][57][58][59]. These representative supports, which possess unique chemical and physical properties, such as controllable release of ion activator and synergic catalysts and response to external stimuli, are able to regulate the enzyme-support interaction and eventually lead to an unprecedented enhancement in immobilized enzyme activity [7,60,61].Overall, recent years have witnessed great success in the interactions between artificial nanostructured supports and natural enzymes for enhanced activity. This review will focus on recent advances in this field in the past 10 years, with an emphasis on various mechanisms behind the boosted catalytic activities, including reduced mass transfer limitation, interfacial ion activation, local heating effect, synergistic effects, conformational changes, substrate channeling and so on. A better understanding of the relationship between the characteristics of the nanostructured supports and the enhanced activities of nanobiocatalysts, may provide new insights in designing efficient nanobiocatalysts for various applications. Mechanisms behind Enhanced Activities of NanobiocatalystsAn overview of recently reported nanobiocatalyst...

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Pursuing the Promise of Enzymatic Enhancement with Nanoparticle Assemblies

Cited by 51 publications

References 146 publications

Quantum Dots and Gold Nanoparticles as Scaffolds for Enzymatic Enhancement: Recent Advances and the Influence of Nanoparticle Size

Quantum Dots and Gold Nanoparticles as Scaffolds for Enzymatic Enhancement: Recent Advances and the Influence of Nanoparticle Size

Transducing Protease Activity into DNA Output for Developing Smart Bionanosensors

Recent Advances in Enzyme-Nanostructure Biocatalysts with Enhanced Activity

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