Mimicking Peroxidase Activities with Prussian Blue ... - ACS Publications

Subscriber access provided by NEW YORK UNIV

Communication

Mimicking Peroxidase Activities with Prussian Blue Nanoparticles and Their Cyanometalate Structural Analogs Margarita Vázquez-González, Rebeca M. Torrente-Rodríguez, Anna Kozell, Wei-Ching Liao, Alessandro Cecconello, Susana Campuzano, Jose M. Pingarron, and Itamar Willner Nano Lett., Just Accepted Manuscript • DOI: 10.1021/acs.nanolett.7b02102 • Publication Date (Web): 28 Jun 2017 Downloaded from http://pubs.acs.org on June 29, 2017

Just Accepted “Just Accepted” manuscripts have been peer-reviewed and accepted for publication. They are posted online prior to technical editing, formatting for publication and author proofing. The American Chemical Society provides “Just Accepted” as a free service to the research community to expedite the dissemination of scientific material as soon as possible after acceptance. “Just Accepted” manuscripts appear in full in PDF format accompanied by an HTML abstract. “Just Accepted” manuscripts have been fully peer reviewed, but should not be considered the official version of record. They are accessible to all readers and citable by the Digital Object Identifier (DOI®). “Just Accepted” is an optional service offered to authors. Therefore, the “Just Accepted” Web site may not include all articles that will be published in the journal. After a manuscript is technically edited and formatted, it will be removed from the “Just Accepted” Web site and published as an ASAP article. Note that technical editing may introduce minor changes to the manuscript text and/or graphics which could affect content, and all legal disclaimers and ethical guidelines that apply to the journal pertain. ACS cannot be held responsible for errors or consequences arising from the use of information contained in these “Just Accepted” manuscripts.

Nano Letters is published by the American Chemical Society. 1155 Sixteenth Street N.W., Washington, DC 20036 Published by American Chemical Society. Copyright © American Chemical Society. However, no copyright claim is made to original U.S. Government works, or works produced by employees of any Commonwealth realm Crown government in the course of their duties.

Page 1 of 17

1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Nano Letters

Mimicking Peroxidase Activities with Prussian Blue Nanoparticles and Their Cyanometalate Structural Analogs Margarita Vázquez-González,† Rebeca M. Torrente-Rodríguez,‡ Anna Kozell, † Wei-Ching Liao,† Alessandro Cecconello, † Susana Campuzano,‡ José M. Pingarrón,‡ Itamar Willner*, † †

Institute of Chemistry, The Center for Nanoscience and Nanotechnology, The Hebrew

University of Jerusalem, Jerusalem 91904, Israel. ‡

Department of Analytical Chemistry, Complutense University of Madrid, Madrid E-28040,

Spain. *E-mail: [email protected]. Tel: 972-2-6585272. Fax: 972-2-6527715

ABSTRACT: Nanoparticles composed of Prussian Blue, PB, and the cyanometalate structural analogs, CuFe, FeCoFe , and FeCo, are examined as inorganic clusters that mimic the functions of peroxidases. PB acts as superior catalyst for the oxidation of dopamine by H2O2 to aminochrome. The oxidation of dopamine by H2O2 in the presence of PB is 6-fold faster than in the presence of CuFe. The cluster FeCo do not catalyze the oxidation of dopamine to aminochrome.

The most efficient catalyst for the generation of chemiluminiscence by the

ACS Paragon Plus Environment

1

Nano Letters

1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Page 2 of 17

oxidation of luminol by H2O2 is, however, FeCo, and PB lacks any catalytic activity toward the generation of chemiluminescence. The order of catalyzed chemiluminescence generation is FeCo >> CuFe > FeCoFe. The clusters PB, CuFe, FeCoFe, and FeCo mimic the functions of NADH peroxidase. The catalyzed oxidation of NADH by H2O2 to form NAD+ follows the order PB>> CuFe ~ FeCoFe, FeCo. The efficient generation of chemiluminescence by the FeCo catalyzed oxidation of luminol by H2O2 is used to develop a glucose sensor. The aerobic oxidation of glucose in the presence of glucose oxidase, GOx, yields gluconic acid and H2O2. The chemiluminescence intensities formed by the GOx-generated H2O2 relate to the concentration of glucose, thus, providing a quantitative readout signal for the concentrations of glucose.

KEYWORDS: NADH, chemiluminescence, dopamine, sensor, catalysis.

Recent research efforts are directed toward the use of supramolecular complexes and inorganic nanomaterials1–3 as catalysts mimicking peroxidases,4,5 and particularly horseradish peroxidase. Different metal oxide nanoparticles, e.g., Fe2O3 nanoparticles,6–8 metal nanoparticles, such as Au9,10 or Cu11,12 nanoparticles, Cu2+ modified graphene oxide13 or Cu2+-functionalized carbon dots14 were reported to mimic functions of horseradish peroxidase. Using some of these nanoparticles, several chemical transformations characteristic to different peroxidases were demonstrated, such as the generation of chemiluminescence13,14 in the presence of luminol and H2O2, the catalyzed oxidation of dopamine to aminochrome13,14 or the catalyzed oxidation of NADH to NAD+ by H2O2 (NADH peroxidase mimicking catalyst).13 Different applications of such catalytic nanoparticles (NPs) may be envisaged including their use for the development of amplified sensing platforms,15,16 bioimaging applications and their use to regenerate the NAD+ in


2

Page 3 of 17

1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Nano Letters

biotechnological processes. In the present study, we introduce Prussian Blue Nanoparticles, PB NPs, Fe1.33Fe(CN)6 NPs and their structural analogs Cu1.33[Fe(CN)6]0.667, CuFe NPs; Fe[Co0.2Fe0.8(CN)6], FeCoFe NPs and FeCo0.67(CN)4, FeCo NPs as peroxidase mimicking catalysts. We reveal that the Prussian Blue NPs and Prussian Blue-like NPs reveal different activities toward the chemical transformations characteristic to peroxidase. The chemical transformations that are addressed in the study include the catalyzed oxidation of dopamine by H2O2 to yield aminochrome, the catalyzed generation of chemiluminescence by luminol/H2O2, and the catalyzed oxidation of NADH to NAD+ by H2O2. We demonstrate that we cannot identify a superior versatile PB or PB-like NPs peroxidase-mimicking catalyst for all of the transformations and the catalytic activities of the different NPs are dictated by the specific chemical processes. Furthermore, we use the peroxidase mimicking functions of FeCo NPs to develop an optical sensor for glucose. The preparation of the PB NPs17 and of the structural analogs18 CuFe, FeCoFe and FeCo NPs followed reported procedures. Figure 1 depicts the SEM and TEM images of the PB and FeCo NPs (the SEM and TEM images of the CuFe and FeCoFe NPs are presentend in Figure S1). The size of the PB NPs is in the range of 40-50 nm while the other NPs reveal a broad size distribution, 100-200 nm. The X-ray diffraction patterns of the PB NPs and all the other cyanometalate structural analogs are similar (see Figure S2), indicating a face centered cubic structure, space group Fm3m. Inductively coupled plasma optical emission spectroscopy measurements (ICP-OES) indicate the following metal-ion percentage in the different NPs: PB NPs (35 % Fe), CuFe NPs (Fe 21.5 %; Cu 17.8 %), FeCoFe NPs (Fe 19.5 %, Co 15.8 %), FeCo NPs (Fe 13.5 %, Co 17.1 %). The absorbance spectra of the different NPs are provided in Figure S3.


3

Nano Letters

1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Page 4 of 17

The PB, CuFe, FeCoFe and FeCo NPs were, then, applied as catalysts for the oxidation of dopamine to aminochrome by H2O2, Figure 2(A). The time-dependent oxidation of dopamine to aminochrome using PB NPs is shown in Figure 2(B). Increasing the NPs concentration results in the enhanced of the oxidation of dopamine. Figure 2(C) shows the absorption spectra of the resulting aminochrome formed after a fixed time interval of 2 h, using a fixed concentration of the PB NPs, and variable concentrations of dopamine. As the concentration of dopamine increases, the catalytic oxidation of dopamine is intensified. Figure 2(D) depicts the timedependent absorbance changes (of aminochrome) upon oxidation of dopamine using variable concentrations of dopamine and a fixed concentration of PB NPs. Similar experiments were performed with the CuFe, FeCoFe and FeCo NPs (results presented in Figure S4 and Figure S5). Figure 2(E) compares the oxidation rates of dopamine to aminochrome by the different NPs. In these experiments, an identical concentration of the NPs was used. Evidently, the PB NPs reveal substantially enhanced catalytic functions toward oxidation of dopamine by H2O2 to form aminochrome (PB, Vmax = 22 µM min-1; CuFe, Vmax = 3.4 µM min-1; FeCoFe, Vmax = 1.6 µM min-1; FeCo, Vmax = 0.2 µM min-1). Furthermore, control experiments revealed that all the components are essential to drive the oxidation of dopamine to aminochrome. The PB NPs and their structural analogs were further examined as catalysts mimicking the horseradish peroxidase catalyzed formation of chemiluminescence through the oxidation of luminol by H2O2. For example, the chemiluminescence spectra generated by different concentrations of FeCo NPs are shown in Figure 3(A). The chemiluminescence spectra are intensified as the concentration of the FeCo NPs increase. The chemiluminescence intensities are controlled by the concentration of H2O2, Figure 3(B). As the concentration of H2O2 increases the chemiluminescence spectra are intensified. Figure 3(B), inset, shows the calibration curve


4

Page 5 of 17

1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Nano Letters

showing the chemiluminescence intensities at λ = 425 nm, as a function of variable concentrations of H2O2. We find that the superior catalyst for the generation of chemiluminescence is the FeCo NPs. Figure 3(C) depicts the chemiluminescence spectra generated by the different NPs. While CuFe and FeCoFe NPs show poor chemiluminescence generation properties (see Figure S6), we find that PB NPs lack any catalytic activity to generate chemiluminescence. It is certainly of interest to understand the origin for the efficient generation of chemiluminescence by the FeCo NPs in contrast to the poor, or even the lack of chemiluminescence activity of the CuFe, FeCoFe NPs and PB NPs, respectively. We speculated that the later NPs quench the excited aminophthalatic acid that is the reactive specie for the generation of chemiluminescence. Accordingly, we used the classical horseradish peroxidase (HPR)-mediated chemiluminescence generation system in the presence of luminol/H2O2 as reference system to probe the possible quenching of the chemiluminescence generating species by the HRP-luminol system. Figure S7, curve (a) depicts the chemiluminescence formed by the HRP-luminol/H2O2 system. Figure S7, curves (b), (c) and (d) shows the chemiluminescence spectra of HRP-luminol/H2O2 system upon addition of PB, CuFe and FeCoFe NPs, respectively. Evidently, the chemiluminescence of HRP-luminol/H2O2 is totally quenched upon addition of the PB NPs, and is strongly quenched by the other two NPs (CuFe and FeCoFe NPs). In contrast, Figure S7, curve (e) shows the chemiluminescence spectrum stimulated by the HRP/H2O2 system upon the addition of the FeCo NPs. Clearly, the chemiluminescence intensity enhanced (~ 2 folds). This is attributed to the fact that the FeCo NPs do not quench the excited aminophthalatic species generated by HRP itself or the excited species generated by the FeCo NPs themselves. The successful quantitative chemiluminescence detection of H2O2 by the FeCo


5

Nano Letters

1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Page 6 of 17

NPs paves the way to apply the NPs as catalytic labels for the detection of the activity of oxidases and their substrates (vide infra). The different kinds of NPs were further examined as catalysts that mimic NADH peroxidase catalyzing the oxidation of NADH by H2O2, Figure 4(A). We find that the four different kinds of NPs catalyze the oxidation of NADH. For example, Figure 4(B) depicts the time-dependent oxidation of different concentrations of NADH by a fixed concentration of PB NPs. As the concentration of NADH increases the rate of oxidation of NADH is faster. Also, the rate of oxidation of NADH is controlled by the concentration of the catalytic NPs. Figure 4 (C) depicts the spectra of the residual NADH upon the H2O2-induced oxidation of NADH, 0.3 mM, by different concentrations of the NPs for a fixed time-interval of 4 h. Evidently, as the concentration of the NPs increases, the oxidation of NADH is enhanced, as reflected by the lower content of residual NADH. Similar experiments using the other NPs are presented in Figure S8. The catalytic effectiveness of the different particles is presented in Figure 4(D). In these experiments we compare the rate of oxidation of NADH to NAD+ using a fixed concentration of NPs. Evidently, we find that the oxidation rate is controlled by the composition of the NPs. Control experiments show that NADH is not oxidized by H2O2 in the absence of the NPs. Also, the free metal ions integrated in the cyanometalate clusters (a similar concentration present in the nanoparticles) do not catalyze the oxidation of NADH by H2O2. A major issue that needs to be addressed in the catalyzed oxidation of NADH by H2O2 relates to the confirmation that NADH is indeed oxidized to NAD+, rather than to the biologically inactive NAD-dimer, (NAD)2. This is particularly important since the H2O2 catalyzed oxidation of NADH to NAD+ may provide a general route for the regeneration of NAD+, and thus may act as a versatile means to drive chemical transformations by NAD+-


6

Page 7 of 17

1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Nano Letters

dependent enzymes.19–23 To confirm the formation of NAD+ as the oxidation product of NADH we coupled the catalytic oxidation of NADH to the NAD+-dependent enzyme alcohol dehydrogenase, AlcDH, that catalyzes the oxidation of alcohols to aldehydes (or ketones). In these experiments, we stimulated the NPs-catalyzed oxidation of NADH by H2O2. After the absorbance of NADH was depleted, ethanol and AlcDH, were added to the system. This resulted in the regeneration of the absorbance of NADH, Figure 5. Note, however, that the absorbance of NADH is slightly lower than the initial absorbance of NADH. This is consistent with the formation of a steady-state equilibrium of NAD+/NADH in the presence of AlcDH/ethanol. These results imply that the oxidation product generated by the oxidation of NADH is the biologically active NAD+ cofactor and not the biological inactive (NAD)2 dimer. The chemiluminescence generated by the FeCo NPs in the presence of luminol/H2O2 provides a means to design optical sensors for substrates that are aerobically catalytically oxidized while generating H2O2 (e.g., glucose/glucose oxidase; lactate/lactate oxidase; choline/choline oxidase). This is exemplified here with the development of glucose sensor using the FeCo NP as a chemiluminescence generation probe, Figure 6(A). The aerobic oxidation of glucose yields gluconic acid and H2O2. Since the concentration of the resulting H2O2 is controlled by the concentration of glucose, the resulting chemiluminescence intensities are related to the concentration of glucose. Accordingly, aqueous samples consisting of a fixed concentration of glucose oxidase, GOx, were allowed to react under aerobic conditions with different concentrations of glucose for a fixed time-interval of 30 min. The mixtures were then subjected to the FeCo NPs and luminol detection system. Figure 6(B) depicts the chemiluminescence intensities generated by the different concentrations of glucose. As the concentration of glucose is higher, the resulting chemiluminescence is intensified. Figure 6(B),


7

Nano Letters

1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Page 8 of 17

inset, shows the resulting calibration curve. That is, upon increasing the concentration of glucose, the amount of GOx-generated H2O2 is higher, resulting in an intensified chemiluminescence output. In conclusion, the present study has introduced Prussian Blue NPs and its structural analogs, CuFe, FeCo and FeCoFe NPs as peroxidase mimicking catalysts. Specifically, we demonstrated that the NPs acted as horseradish peroxidase mimicking catalysts reflected by the catalyzed H2O2-driven oxidation of dopamine to aminochrome and by the H2O2 catalyzed oxidation of luminol with generation of chemiluminescence. Also, the different NPs acted as NADH peroxidase mimicking catalysts that catalyzed the H2O2 oxidation of NADH to NAD+. We find that the peroxidase mimicking functions of the different NPs are controlled by the composition of the NPs.

We demonstrated that PB NPs lack catalytic peroxidase-mimicking

chemiluminescence generating functions and CuFe and FeCoFe NPs showed poor catalytic chemiluminescence

generation

properties,

but

the

FeCo

NPs

revealed

efficient

chemiluminescence generation properties in the presence of luminol/H2O2. Beyond the significance of the study in introducing a broad class of inorganic clustered NPs as peroxidase mimicking materials, the study reveals possible applications of these catalytic materials. The regeneration of the NAD+ cofactor by the NPs could be coupled to various chemical transformations involving NAD+-dependent enzymes. Also, by using different NPs as catalytic optical labels for the development of sensors for substrates of oxidases or NAD+-dependent enzymes is feasible. Furthermore, a recent study24 has addressed the use of PB NPs as catalyst mimicking three antioxidant enzymes (peroxidase, superoxide dismutase and catalase) active as Reactive Oxygen Species (ROS) degradation biocatalysts. The different catalytic activities of the cyanometalate nanoparticles, demonstrated in the present study, suggest that these NPs could


8

Page 9 of 17

1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Nano Letters

reveal diverse antioxidant features toward ROS, thereby having important implications for nanomedicine and particularly cell apoptosis.

Figure 1. (A) TEM and (B) SEM images of the PB NPs. (C) and (D) correspond to TEM and SEM images of the FeCo NPs.


9

Nano Letters

1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Page 10 of 17

Figure 2: (A) Schematic PB NPs-catalyzed oxidation of dopamine by H2O2 to yield aminochrome. (B) Rates of oxidation of different concentrations of dopamine to aminochrome by H2O2 in the presence of different concentrations of PB NPs: (a) 1, (b) 5, (c) 10 µg mL-1. In all experiments [H2O2] = 2 mM. (C) Absorption spectra corresponding to the aminochrome generated by the PB NPs-catalyzed oxidation of different concentrations of dopamine using [H2O2] = 2 mM, [PB NPs] = 10 µg mL-1 and a fixed time of reaction corresponding to 2 h. Dopamine concentrations corresponding to (a) 0, (b) 0.05, (c) 0.1, (d) 0.25, (e) 0.5, (f) 1 mM. (D) Time-dependent absorbance changes upon oxidation of different concentrations of dopamine by H2O2 to form aminochrome. Dopamine concentrations correspond to (a) 0, (b) 0.05, (c) 0.1, (d) 0.25, (e) 0.5, (f) 1 mM. In all experiments, [PB NPs] = 10 µg mL-1; [H2O2] = 2 mM. (E) Rates of oxidation of different concentrations of dopamine to aminochrome using different cyanometalate NPs (10 µg mL-1): (a) FeCo, (b) FeCoFe, (c) CuFe, (d) PB NPs. In all experiments [H2O2] = 2 mM.


10

Page 11 of 17

1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Nano Letters

Figure 3. (A) Chemiluminescence spectra generated by the FeCo NPs-catalyzed oxidation of luminol by H2O2 in the presence of different concentrations of the NPs: (a) 25, (b) 50, (c) 100 µg mL-1. In all experiments [luminol] = 0.5 mM, [H2O2] = 0.1 mM. Inset: Schematic FeCo NPscatalyzed generation of chemiluminescence. (B) Chemiluminescence spectra generated by the FeCo NPs, 100 µg mL-1 in the presence of luminol, 0.5 mM, and using variable concentration of H2O2: (a) 0, (b) 0.01 (c) 0.025, (d) 0.05, (e) 0.075 (f) 0.1 mM. Inset: Derived calibration curve. (C) Chemiluminescence spectra generated by: (a) PB, (b) FeCoFe, (c) CuFe, (d) FeCo NPs. In all experiments: [luminol]= 0.5 mM, [H2O2] = 0.1 mM and [NPs] = 100 µg mL-1.


11

Nano Letters

1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Page 12 of 17

Figure 4: (A) Schematic PB NPs catalyzed oxidation of NADH to NAD+ by H2O2. (B) Timedependent absorbance changes corresponding to the PB NPs catalyzed oxidation of NADH by H2O2 using different concentrations of NADH: (a) 0, (b) 0.05, (c) 0.1, (d) 0.2, (e) 0.3, (f) 0.4, (g) 0.5 mM. In all experiments, [PB NPs] = 10 µg mL-1; [H2O2] = 2 mM. (C) Absorbance spectra of the residual NADH upon treatment of NADH, 0.3 mM, with H2O2, 2 mM, by variable amounts of PB NPs for a fixed time-interval of 4h: (a) No added PB (b) 1, (c) 5, (d) 10 µg mL-1 PB NPs. (D) Rates of oxidation of different concentrations of NADH by H2O2 in the presence of the different cyanometalate catalysts: (a) FeCo, (b) CuFe, (c) FeCoFe, (d) PB NPs. In all experiments, the concentration of the NPs corresponded to 10 µg mL-1, and H2O2, 2 mM.


12

Page 13 of 17

1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Nano Letters

Figure 5. Time-dependent absorbance changes upon the PB NPs-catalyzed oxidation of NADH by H2O2 to form NAD+ and the subsequent AlcDH/ethanol regeneration of NADH. Arrow marks the time when AlcDH/ethanol was added to the system. Inset: PB NPs-catalyzed oxidation of NADH to NAD+ by H2O2 as a regeneration cycle for the operation of NAD+-dependent enzymes (described for alcohol dehydrogenase, AlcDH, that oxidizes ethanol to acetaldehyde).

Figure 6: Coupling of the FeCo NPs catalyzed chemiluminescence generation system to the GOx-mediated aerobic oxidation of glucose to gluconic acid and H2O2 for the development of a glucose sensor. (B) Chemiluminescence spectra generated by the system shown in (A) using different concentrations of glucose: (a) 0, (b) 0.1, (c) 0.25, (d) 0.5, e) 1 mM . Inset: Derived calibration curve.


13

Nano Letters

1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Page 14 of 17

ASSOCIATED CONTENT Supporting Information. A detail list of the materials, synthetic procedures to prepare the different NPs and the composition of the different samples are provided in the supporting information. Also, additional SEM/TEM images of NPs not shown in the main text and the results of some experiments discussed in the text are provided in the supporting information. This material is available free of charge on ACS Publications website. AUTHOR INFORMATION Corresponding Author *E-mail: [email protected]. Tel: 972-2-6585272. Fax: 972-2-6527715. Author Contributions All authors participated in the formulation of the paper and all have given their approval to this form of the manuscript Notes The authors declare no competing ﬁnancial interest. ACKNOWLEDGMENTS This study is supported by The Minerva Center for Biohybrid Complex Systems. R.M.T-R acknowledges a predoctoral contract from the Spanish Ministerio de Economía y Competitividad (Reserch Project CTQ-2015-64402-C2-1-R).


14

Page 15 of 17

1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Nano Letters

REFERENCES (1) J. T. Groves, R. C. Haushalter, M. Nakamura, T. E. Nemo, B. J. Evans, J. Am. Chem. Soc. 1981, 103, 2884-2886. (2) P. Travascio, Y. Li, D. Sen, Chem. Biol. 1998, 5, 505-517 (3) P. Travascio, A. J. Bennet, D. Y. Wang, D. Sen, Chem. Biol. 1999, 6, 779-787. (4) R. Schlögl, Angew. Chem. Int. Ed. 2015, 54, 3465-3520. (5) A. Asati, S. Santra, C. Kaittanis, S. Nath, J. M. Perez, Angew. Chem. Int. Ed. 2009, 48, 23082312. (6) L. Gao, J. Zhuang, L. Nie, J. Zhang, Y. Zhang, N. Gu, T. Wang, J. Feng, D. Yang, S. Perrett, X. Yan, Nat. Nanotech. 2007, 2, 577-583. (7) R. Ragg, M. N. Tahir, W. Tremel, Eur. J. Inorg. Chem. 2016, 2016, 1906-1915. (8) H. Wei, E. Wang, Anal. Chem. 2008, 80, 2250-2254. (9) M. Comotti, C. Della Pina, R. Matarrese, M. Rossi, Angew. Chem. Int. Ed. 2004, 43, 58125815. (10) X. Zheng, Q. Liu, C. Jing, Y. Li, D. Li, W. Luo, Y. Wen, Y. He, Q. Huang, Y-T. Long, C. Fan, Angew. Chem. Int. Ed. 2011, 50, 11994-11998. (11) M. B. Gawande, A. Goswami, F.-X. Felpin, T. Asefa, X. Huang, R. Silva, X. Zou, R. Zboril, R. S. Varma, Chem. Rev. 2016, 116, 3722-3811. (12) X. Kang, Z. Mai, X. Zou, P. Cai, J. Mo, Anal. Biochem. 2007, 363, 143-150. (13) S. Wang, R. Cazelles, W.-C. Liao, M. Vázquez-González, A. Zoabi, R. Abu-Reziq, I. Willner, Nano Lett. 2017, 17, 2043-2048. (14) M. Vázquez-González, W.-C. Liao, R. Cazelles, S. Wang, X. Yu, V. Gutkin, I. Willner, ACS Nano 2017, 11, 3247-3253. (15) Y. Xiao, V. Pavlov, R. Gill, T. Bourenko, I. Willner, ChemBioChem. 2004, 5, 374-379. (16) V. Pavlov, Y. Xiao, R. Gill, A. Dishon, M. Kotler, I. Willner, Anal. Chem. 2004, 76, 21522156. (17) M. Shokouhimehr, E. S. Soehnlen, J. Hao, M. Griswold, C. Flask, X. Fan, J. P. Basilion, S. Basu, S. D. Huang, J. Mater. Chem. 2010, 20, 5251-5259. (18) W. Wang, J. Feng, Y. Ye, F. Lyu, Y.-S. Liu, J. Guo, Y. Yin, Nano Lett. 2017, 17, 755-761. (19) R. DiCosimo, C.-H. Wong, L. Daniels, G. M. Whitesides, J. Org. Chem. 1981, 46, 46224623. (20) Z. Shaked, G. M. Whitesides, J. Am. Chem. Soc. 1980, 102, 7104-7105.


15

Nano Letters

1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Page 16 of 17

(21) B. R. Riebel, P. R. Gibbs, W. B. Wellborn, A. S. Bommarius, Adv. Synth. Catal. 2003, 345, 707-712. (22) X. Wang, H. H. P. Yiu, ACS Catal. 2016, 6, 1880-1886. (23) J. Liu, M. Antonietti, Energy Environ. Sci. 2013, 6, 1486-1493. (24) W. Zhang, S. Hu, J.-J. Yin, W. He, W. Lu, M. Ma, N. Gu, Y. Zhang, J.Am. Chem. Soc. 2016, 138, 5860-5865.


16

Page 17 of 17

1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60

Nano Letters

BRIEFS Prussian Blue nanoparticles and its cyanometalate structural analog nanoparticles reveal different catalytic activities mimicking peroxidases. The effective chemiluminescence generated by the FeCo cyanometalate cluster nanoparticles are applied to develop a glucose sensor. FOR TABLE OF CONTENTS ONLY


17

Mimicking Peroxidase Activities with Prussian Blue ... - ACS Publications

Recommend Documents