Fe-porphyrin-based covalent organic framework as a novel

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Fe-porphyrin-based covalent organic framework as a novel peroxidase mimic for one-pot glucose colorimetric assay Zhihui Dai, Junning Wang, Xue Yang, Tianxiang Wei, Jianchun Bao, and Qinshu Zhu ACS Appl. Bio Mater., Just Accepted Manuscript • DOI: 10.1021/acsabm.8b00104 • Publication Date (Web): 11 Jul 2018 Downloaded from http://pubs.acs.org on July 11, 2018

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ACS Applied Bio Materials

Fe-porphyrin-based covalent organic framework as a novel peroxidase mimic for one-pot glucose colorimetric assay Junning Wanga, Xue Yanga, Tianxiang Weia, Jianchun Baoa, Qinshu Zhu*b and Zhihui Dai*a,b a. Jiangsu Key Laboratory of Biofunctional Materials, School of Chemistry and Materials Science, Nanjing Normal University, Nanjing 210023, P. R. China b. Nanjing Normal University Centre for Analysis and Testing, Nanjing, 210023, P. R. China *Corresponding author. E-mail address: [email protected] and [email protected]; Tel/Fax: +86-25-85891051

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ABSTRACT:. Covalent organic frameworks (COFs) have recently emerged as very fascinating porous polymers due to their attractive design synthesis and various applications. However, the catalytic application of COF materials as enzymatic mimics remains largely unexplored. In this work, Fe-porphyrin-based covalent organic framework (Fe-COF) has been successfully synthesized through a facile post-synthetic strategy for the first time. In the presence of hydrogen peroxide (H2O2), Fe-COF can catalyze chromogenic substrate (3,3′,5,5′-tetramethylbenzidine (TMB)) to produce color, and this just goes to show that it has inner peroxidase-like activity. Moreover, the kinetic studies indicate that the Fe-COF nanomaterial has higher affinity towards both the substrate H2O2 and TMB than the natural enzyme, horseradish peroxidase (HRP). Under the optimized conditions, the Fe-COF nanomaterial was applied in a colorimetric sensor for the sensitive detection of H2O2. The detection range was from 7 to 500 µM, and the detection limit was 1.1 µM. Furthermore, the combination of Fe-COF with glucose oxidase (GOx) can be implemented to measure glucose by a one-pot method, and the obtained detection range was 5 to 350 µM and the detection limit was 1.0 µM. It was proved that the sensor can be successfully used to detect the concentration of glucose in human serum samples. As a peroxidase mimic, FeCOF exhibits the advantages of easy preparation, good stability and ultrahigh catalytic efficiency. We believed that the proposed method in this work would facilitate the applications of COF-based composites as enzymatic mimics in biomedical fields.

KEYWORDS: covalent organic frameworks, peroxidase mimic, one-pot, colorimetric assay, glucose


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INTRODUCTION In recent years, colorimetric methods have drawn much attention for field analysis and pointof-care diagnosis applications.1−3 They offer the merits of simplicity, practicality, rapidity, and do not need any expensive or sophisticated instrumentation. Among them, the colorimetric method based on enzyme catalysts has attracted much attention due to its high catalytic efficiency and rapidity of catalytic reaction. However, because the applications of natural enzymes are usually restricted due to storage difficulties, instability and complicated preparation and purification process,4,5 the development of biomimetic catalysis especially nanomaterialsbased enzyme mimic with high stability, high catalytic activity and high substrate specificity by facile strategies is very necessary.6,7 Recently, metal–organic frameworks (MOFs), as a new class of materials with peroxidase-like activity, have been successfully explored for colorimetric sensors due to their permanent porosity, high stability and high surface area.8−10 For example, MIL-53 (Fe),8 Ce-MOF,9 and Fe3O4@MIL-100 (Fe),10 have been reported to show peroxidaselike catalytic activity and applied to colorimetric assays for the detection of H2O2, AA and glucose. Covalent organic frameworks (COFs), which are connected by strong covalent bonds between the components−the light-weight elements, such as carbon, boron, nitrogen and oxygen, into ordered structures with atomic precision, have emerged as another new class of crystalline organic porous materials.11−13 Due to their porosity, low density, high thermal stability and topologically designable structure, COFs have shown great potential applications in sensing,14 gas storage,15 especially in catalytic fields.16 Moreover, COFs have more unique advantages than other crystalline porous materials, particularly in post-synthetic modification which can introduce different functional groups easily. Based on the post-synthesis strategy, various studies


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in catalysis using COFs have been reported.16−18 The application of COF materials in catalysis has been reported for the first time by Wang and co-workers.16 They synthesized a Pd/COFLZU-1 material via a simple post-synthesis strategy. As its unique structure provided the accessibility of active sites and the simplification for diffusing into the bulky products, this material showed excellent activity in the Suzuki-Miyaura coupling reaction. Over the last few years, some attempts were performed by loading metal nanoparticles into COFs by posttreatment, resulting in enhanced reactivity in chemical reactions such as nitro reduction,19 glycerol oxidation,20 Heck-Sonogashira coupling21 and water oxidation electrocatalyst.18 However, there are very few reports on the catalytic application of COF materials as enzyme mimic. Currently, porphyrins-based COFs, which consist of π–π stacking of porphyrin units in the adjacent layers, have potential application in catalysis fields.22,23 As a component of hemoglobin, porphyrins consist of abundant functionalized nitrogen groups. Due to their particular construction, porphyrins can be metalated via pre- and post-metalation methods. As is wellknown, the metalated porphyrins can be potentially applied to gas adsorption and catalytic reaction.24,25 Besides, HRP and heme, which contain Fe2+ or Fe3+ in their reaction centers, have been proved to have inherent peroxidase-like activity.26 With this background in mind, a Fe-porphyrin-based COF (Fe-COF) material was synthesized by a facile post-synthetic strategy. To our surprise, kinetic studies indicate that the Fe-COF had higher affinity towards both the substrate H2O2 and TMB than the natural enzyme, HRP. We then applied Fe-COF as an enzyme-mimic for the detection of H2O2 in a colorimetric assay, a relatively wide detection range (7 to 500 µM) and a low detection limit (1.1 µM) were obtained. Combining it with GOx, the sensitive quantitative determination of glucose by a one-pot


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colorimetric test was also achieved, and the obtained detection range was 5 to 350 µM and the detection limit was 1.0 µM. On the basis of its excellent peroxidase mimic’s catalytic activity and the particular construction, the Fe-COF was successfully applied to the determination of glucose in human serum samples by a one-pot colorimetric method. These applications of our proposed Fe-COF material show tremendous potential of COF-based composites as enzymatic mimics in biomedical fields. EXPERIMENTAL SECTION Preparation of Fe-COF. FeSO4⋅7H2O (12.5 mg, 0.05 mmol) and COF-366 (10.0 mg) were dissolved in a 6 mL mixture of dichloromethane and methanol. The mixture was stirred continuously for 36 h at room temperature. The resulting solid was separated by centrifugation, washed with dichloromethane and methanol, and then put the solid in the vacuum drying oven (60 °C, 12 h) in order to obtain product (Fe-COF, brown powder, 18 mg, 80% yield). Fe content was 8.49 % from ICP analyses. IR (KBr, cm−1): 3460, 1620, 1514, 1471, 1426, 1384, 1292, 1233, 1151, 1112, 798, 615, 440. Kinetic analysis. The assay was conducted at 40 °C by mixing Fe-COF (90 µg mL−1), TMB and H2O2 in NaAc buffer solution (pH 5). If the concentration of H2O2 remains unchanged, then change the concentration of TMB, and vice versa. Kinetic parameters (maximum reaction rate (Vmax), Michaelis constant (Km)) could be achieved by the following Line-weaver–Burk plot: 1/ν = (Km/Vmax)⋅(1/[S]+1/Km),27 where ν stands for the initial rates of the reaction, [S] the concentration of substrate (TMB or H2O2). Detection of H2O2 and glucose using Fe-COF as peroxidase mimics. The steps of detection of H2O2 by colorimetric assay are as follows: first, adding Fe-COF (90 µg mL−1), TMB (1 mM)


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and different concentrations of H2O2 into 350 µL acetate buffer (0.2 M, pH 5). Second, measuring the absorbance at 652 nm (reaction time: 20 min). The quantitative detection of glucose was performed by a one-pot detection using GOx and FeCOF. The reactions were conducted in solution containing 175 µL NaAc buffer solution (pH 5), 50 µL TMB (1 mM), 100 µL Fe-COF (45 µg mL−1), 125 µL GOx (2 mg/mL) and together with different concentrations of glucose, at 40 °C for 20 min. RESULTS AND DISCUSSION Characterization of Fe-COF. As can be seen from Figure 1, the mean size distribution of FeCOF in nanometer-regime was characterized by SEM. The comparison of the morphology of the COF-366 and Fe-COF proves that the framework structure of COF-366 retained intact (Figure 1A and 1B). The thermogravimetric analysis (TGA) curve shows the weight loss (Figure S1) of COF-366, corresponding to the previous reports.22 From Figure S1 we can see that COF-366 begins to lose its weight at 400 °C and the TGA curve of Fe-COF shows that it is stable until 350 °C. The FT-IR spectra of COF-366 and Fe-COF samples are displayed in Figure 1C. And the FTIR spectrum of Fe-COF shows that the original chemical functional groups of COF-366 still exist. However, compared with the FTIR of COF-366, the spectrum of Fe-COF shows a red shift and a broad ν C−N peak, which verifies the coordination bond formation between Fe and N atoms of COF-366 structure. In addition, the FTIR spectrum of Fe-COF in the porphyrin area is almost identical to that of COF-366, indicating the structural retention of COF-366 after the posttreatment. As shown in Figure 1D, the XRD pattern of COF-366 shows intense peaks at 2θ of 3.5°, which corresponds to the previous report.22 The certain accordance between the XRD patterns of COF-366 and Fe-COF suggests that the original chemical functional groups of COF366 still exist in Fe-COF. The wide-range XPS spectra show that COF-366 only contains O, N


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and C element, and Fe-COF contains O, N, C, S and Fe, which confirm the existence of Fe element (Figure S2). Moreover, the XPS spectrum of Fe 2p can be divided into four peaks (Figure 2). Two of the peaks appear at 724.2 eV and 712.2 eV, which can be pointed to Fe(III), the other two peaks are located at 722.6 eV and 709.6 eV, which can be attributed to Fe(II).28−31 Taken together, these results suggest that Fe-COF nanocomposite is successfully fabricated.

Figure 1. The SEM images of COF-366 (A) and Fe-COF (B); (C) The FTIR spectra of (a) COF366, (b) Fe-COF, (c) TAPP and (d) terephthal dehyde. (D) The XRD patterns of (a) COF-366 and (b) Fe-COF.


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Figure 2. The Fe 2p XPS spectra of Fe-COF. Peroxidase-like activity of Fe-COF. TMB is a chromogenic substrate, which can be used to confirm the peroxidase activities of some enzymes (ribozyme,32 DNAzyme33) and nanomaterials.34 The catalytic performance of the synthesized Fe-COF, which can oxidize chromogenic substrate TMB in the presence of hydrogen peroxide, is proved as follows. The oxidation product of TMB is blue and its characteristic absorbance is 652 nm.35 The composite material of Fe-COF is used for the peroxidase-like activity detection, while pristine COF-366 material is used as control experiments. As shown in Figure 3, the mixture solution of TMB with either COF-366 or H2O2 is colorless, but the solution of Fe-COF, TMB and H2O2 is blue color. The results are exactly consistent with characteristic UV–vis spectra, where the maximum absorbance at 652 nm of Fe-COF system is much higher than those of other systems. Besides, it is important to confirm that the peroxidase-like activity was caused by Fe-COF materials, rather than the leaching of iron ions from the structure of Fe-COF under acidic condition. To verify this, the concentration of iron ions in the supernatant of Fe-COF in different pHs are measured by a colorimetric method.36 Under the condition of pH ≥ 5.0, the absorbance of the supernatants of the Fe-COF solution is almost negligible at 508 nm, indicating that there is little iron ion


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leaching from the Fe-COF material (Figure S3). These results indicate that Fe-COF is capable of catalyzing TMB, similar to other enzyme mimetics and HRP.37,38

Figure 3. UV–vis spectra of (a) TMB + H2O2; (b) TMB + COF-366; (c) TMB + H2O2 + COF366; (d) TMB + Fe-COF and (e) TMB + H2O2 + Fe-COF. Inset, the photographs of the solutions. Conditions: TMB, 1 mM (M = mol L−1); H2O2, 100 µM; Fe-COF, 90 µg mL−1; incubation 20 min in pH 5.0 NaAc buffer at 40 °C. Kinetic analysis. To further analyze the catalytic activity of the Fe-COF, the steady-state kinetic data for the reaction are investigated with H2O2 and TMB as substrates (Figure 4). The kinetic experiments are conducted by fixing one substrate concentration and varying the other substrate concentration. We can use the Lineweaver-Burk plots to calculate the steady-state kinetics fitting parameters of Vmax and Km,39 which are summarized in Table 1. According to Table 1, the Km values of the Fe-COF with TMB and H2O2 are 0.02 mM and 0.143 mM, respectively. It is known that a smaller Km value represents a stronger affinity of enzyme for a substrate. Thus the Km (TMB) and Km (H2O2) for Fe-COF are smaller than those of HRP (Table 1), suggesting that Fe-COF has relatively strong affinity to TMB and H2O2 than natural enzymes. Moreover, the Km (TMB) of Fe-COF is much smaller than those of HRP and other metal–organic frameworks (MOFs)-based peroxidase mimics, indicating that Fe-COF has a much stronger


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affinity towards TMB than those of natural enzymes and other mimics. The superior catalytic activity of Fe-COF material can be originated from its unique structure, which offers accessible active sites and fast diffusion for the small analytes and large enzyme.

Figure 4. Kinetic assay of Fe-COF material. (A) The H2O2 concentration was a constant (10 mM) with varying concentrations of TMB. (C) The concentration of TMB was 1 mM with varying concentrations of H2O2. The double reciprocal plots (B and D) were from MichaelisMenten curves. Table 1. Comparison of the steady-state kinetic fitting parameters Vmax and Km. Vmax/M s−1

Km/mM Catalyst TMB

H2O2

Fe-COF

0.02

0.143 3.83×10−8

4.74×10−8

HRP26

0.434

1.0×10−7

8.71×10−8

Fe3O4@MIL-100(Fe)10 0.112 0.077 1.14×10−7

1.8×10−7

3.7

TMB

H2O2

MIL-53(Fe)8

1.08

0.04

8.78×10−8

1.86×10−8

CuNPs@C40

1.65

1.89

1.21×10−7

5.3×10−8


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Mechanism. Terephthalic acid (TA) was used as a fluorescent probe to investigate the possible catalytic mechanism of Fe-COF. The materials of Fe-COF could catalyze H2O2 to generate hydroxyl radicals (⋅OH), which reacted with TA to generate a product (2-hydroxy terephthalic acid) with fluorescent properties.41 With the increase of the Fe-COF concentration, the fluorescence intensity was also increased (Figure 5). However, the fluorescence intensity couldn't be obviously observed in the absence of Fe-COF. The results verified that H2O2 would be decomposed into ⋅OH radicals under the reaction of Fe-COF. In order to further verify the generation of ⋅OH radicals, 5,5-dimethy-1-pyrroline N-oxide (DMPO) spin trapping Electron spin resonance (ESR) spectroscopy was carried out. As shown in Figure S4, the ESR spectra showed a 4-fold characteristic peaks with intensity of 1:2:2:1, which are attributed to the signal of DMPO-•OH adducts.42 Thus, the inner peroxidase-like activity of Fe-COF could be attributed to the production of ⋅OH radicals from the decomposition of H2O2.43

Figure 5. The fluorescence emission spectra of terephthalic acid in the presence of H2O2 and different concentrations of Fe-COF. The reaction was carried out in acetate buffer (pH 5.0) with 0.5 mM terephthalic acid, 10 mM H2O2 and Fe-COF with different concentrations (a-f : 0, 20, 40, 60 , 80, 90 µg mL−1) at 40 °C for 40 min.


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Robustness of peroxidase activity of Fe-COF. It is well known that experimental conditions such as temperature and concentration affect the catalytic activity of natural enzymes in the practical application.44 On the basis of the previous report, the catalytic activity of enzyme in the condition of pH < 5 or temperatures above 40 °C is weakened significantly.27 However, the asprepared Fe-COF nanomaterial can remain stable after 1.5 h with incubation in different pHs (3−9) and different temperatures (25−55 °C) (Figure 6). Therefore, as a new peroxidase mimic, the stability of Fe-COF is better than natural enzymes. Due to the robustness of Fe-COF nanomaterial, it can be widely applied in the biomedical fields.

Figure 6. Relative catalytic activity of Fe-COF after 1.5 h with incubation in different pHs (3−9) (A) and different temperatures (25−55 °C) (B). The maximum point in each curve was set as 100%. Quantitative determination of H2O2 and glucose. At the optimal experimental conditions (Figure S5), a colorimetric strategy for the quantitative detection of H2O2 was performed using the Fe-COF as the catalyst. As shown in Figure S6, the absorption spectrum increased gradually with increasing H2O2 concentration up to 500 µM. It also exhibited good measurement reproducibility. Moreover, two different linear ranges for detecting H2O2 were from 7 to 30 µM and from 30 to 500 µM with the correlation coefficient of 0.9971 and 0.9945, respectively. The detection limit (DL, 3σ) was calculated to be 1.1 µM, lower than that of other peroxidase mimics


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(Table S1). As we all know, H2O2 could be produced by glucose oxidase (GOx) catalysis. Therefore, the combination of Fe-COF with glucose oxidase (GOx) can be implemented to measure glucose (Scheme 1).

Scheme 1. Schematic representation of colorimetric sensor for glucose detection using the FeCOF as the catalyst The curves of logarithm of glucose concentration−response were shown in Figure 7: the curves displayed two different linear ranges from 5 to 50 µM and from 50 to 350 µM with the equations ∆A = 0.0724 +0.1043 lg ([glucose]/µM) (R2= 0.9913) and ∆A = -0.5584 +0.4695 lg ([glucose]/µM) (R2= 0.9917), respectively. The detection limit of glucose by using the proposed strategy was calculated to be 1.0 µM (3σ rule). Moreover, the previous researches on various glucose detections were used to have a comparative investigation, in which the proposed sensing platform showed comparable or even better sensitivity when compared with previous correlative work (Table S2) as a peroxidase mimic.


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Figure 7. The dose-response curves of the logarithm of the glucose concentration. Inset: the enlarged figure of different linear calibration plots for logarithm of the glucose concentration. To explore the practicability, we try to explore the quantitative determination of glucose concentration in human serum samples. All the samples collected from a local hospital were measured by commercial blood glucose meter. Before using serum samples, the samples were firstly centrifuged for 5 minutes at 3000 rpm, and then collected the supernatant for further use. As we all know, the healthy human’s glucose concentration range is different from that of the diabetes.45 The collected samples contained one healthy sample and two diabetic samples. The glucose concentrations in different human serums were calculated according to calibration curve. As shown in Table 2, the test results obtained by the proposed approach were agreement with that detected by commercial blood glucose meter. In addition, the average recoveries of glucose added into serum samples were found to be 98.6 %, 98.9 %, and 97.9 %. From the results above, this approach has good recovery, accuracy and feasibility for the detection.


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Table 2. Determination of glucose in real samples according to the proposed approach. Proposed method Glucometer

RSD

Human serum sample (mM, n=3)

(mM)

n=3 (%)

Sample 1

5.12 ± 0.12

5.01

2.11

Sample 2

13.57 ± 0.56

13.37

4.02

Sample 3

17.28 ± 0.32

17.4

1.64

Selectivity of the proposed approach. To verify the selectivity of the proposed method to glucose, the responses of the material to several carbohydrates (sucrose, maltose and lactose) were tested. From figure S7, obvious differences in absorption intensities were observed between these carbohydrates and glucose. Moreover, the aforementioned several carbohydrates with 10fold concentration of glucose had no significant absorbance intensity. The results suggest that the developed approach for glucose detection show good selectivity. CONCLUSIONS In summary, we employ the post-synthetic strategy for success in getting Fe-COF nanocomposite for the first time. Furthermore, this kind of materials was proved to have an intrinsic peroxidase-like catalytic activity which was superior to HRP in some aspects, such as stability and catalytic activity. In addition, the peroxidase-like Fe-COF materials showed good selectivity. By using our catalyst and glucose oxidase (GOx), a one-pot colorimetric assay with high sensitivity and selectivity for the detection of glucose was realized. On the basis of these findings, we believed that our work can facilitate the possibility of utilizing COF-based porous composites as enzymatic mimics in bioanalysis and medical diagnostics.


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ASSOCIATED CONTENT Supporting Information Chemicals and materials; apparatus; experimental section; TGA curves; XPS; UV-vis spectra; optimization; linear calibration plot for H2O2; selectivity; analytical performance comparison . AUTHOR INFORMATION Corresponding Author *Tel/Fax: +86-25-8589105. E-mail address: [email protected] and [email protected]; Notes The authors declare no competing financial interest.

ACKNOWLEDGMENT This work was supported by the National Natural Science Foundation of China for the project (21625502, 21475062, 21471081) and PAPD. ABBREVIATIONS COFs, covalent organic frameworks; Fe-COF, Fe-porphyrin-based covalent organic framework; TMB, 3,3′,5,5′-tetramethylbenzidine; HRP, horseradish peroxidase; GOx, glucose oxidase; MOFs, metal–organic frameworks.


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REFERENCES (1) De, M.; Ghosh, P. S.; Rotello, V. M. Applications of Nanoparticles in Biology, Adv. Mater. 2008, 20, 4225–4241. (2) Song, S.; Qin, Y.; He, Y.; Huang, Q.; Fan, C.; Chen, H. Y. Functional Nanoprobes for Ultrasensitive Detection of Biomolecules, Chem. Soc. Rev. 2010, 39, 4234–4243. (3) Song, Y.; Wei, W.; Qu, X. Colorimetric Biosensing Using Smart Materials, Adv. Mater. 2011, 23, 4215–4236 (4) Schmid, A.; Dordick, J. S.; Hauer, B.; Kiener, A.; Wubbolts, M.; Wtholt, B. Industrial Biocatalysis Today and Tomorrow, Nature. 2001, 409, 258–268. (5) Reedy, C. J; Gibney, B. R. Heme Protein Assemblies, Chem. Rev. 2004, 104, 617–649. (6) Lin, Y.; Ren, J.; Qu, X. Catalytically Active Nanomaterials: a Promising Candidate for Artificial Enzymes, Acc. Chem. Res. 2014, 47, 1097–1105. (7) Wei, H.; Wang, E. Nanomaterials with Enzyme-Like Characteristics (Nanozymes): NextGeneration Artificial Enzymes, Chem. Soc. Rev. 2013, 42, 6060–6093. (8) Ai, L. H.; Li, L. L.; Zhang, C. H.; Fu, J.; Jiang, J. MIL-53 (Fe): a Metal–Organic Framework with Intrinsic Peroxidase-Like Catalytic Activity for Colorimetric Biosensing, Chem. Eur. J. 2013, 19, 15105–15108. (9) Xiong, Y.; Chen, S.; Ye, F.; Su, L.; Zhang, C.; Shen, S. F.; Zhao, S. Synthesis of a Mixed Valence State Ce-MOF as an Oxidase Mimetic for the Colorimetric Detection of Biothiols, Chem. Commun. 2015, 51, 4635–4638.


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(10) Wu, Y. Z.; Ma, Y. J.; Xu, G. H.; Wei, F. D.; Ma, Y. S.; Song, Q.; Wang, X.; Tang, T.; Song, Y. Y.; Shi, M. L.; Xu, X. M.; Hu, Q. Metal−Organic Framework Coated Fe3O4 Magnetic Nanoparticles with Peroxidase-Like Activity for Colorimetric Sensing of Cholesterol, Sens. Actuators B. 2017, 249, 195–202. (11) Côté, A. P.; Benin, A. I.; Ockwig, N. W.; O'Keeffe, M.; Matzger, A. J.; Yaghi, O. M. Porous, Crystalline, Covalent Organic Frameworks, Science. 2005, 310, 1166–1170. (12) Feng, X.; Ding, X.; Jiang, D. Covalent Organic Frameworks, Chem. Soc. Rev. 2012, 41, 6010–6022. (13) Waller, P. J.; Gándara, F.; Yaghi, O.M. Chemistry of Covalent Organic Frameworks, Acc. Chem. Res. 2015, 48, 3053–3063. (14) Ding, S. Y.; Dong, M.; Wang, Y. W.; Chen, Y. T.; Wang, H. Z.; Su, C. Y.; Wang, W. Thioether-Based Fluorescent Covalent Organic Framework for Selective Detection and Facile Rremoval of Mercury (II), J. Am. Chem. Soc. 2016, 138, 3031–3037. (15) Zeng, Y. Y.; Zou, R.; Luo, Z.; Zhang, H. C.; Yao, X.; Ma, X.; Zou, R. Q.; Zhao, Y. L.. Covalent Organic Frameworks Formed with Two Types of Covalent Bonds Based on Orthogonal Reactions, J. Am. Chem. Soc. 2015, 137, 1020–1023. (16) Ding, S. Y.; Gao, J.; Wang, Q.; Zhang, Y.; Song, W. G.; Su, C. Y.; Wang, W. Construction of Covalent Organic Framework for Catalysis: Pd/COF-LZU1 in Suzuki–Miyaura Coupling Reaction, J. Am. Chem. Soc. 2011, 133, 19816–19822. (17) Nagai, A.; Guo, Z. Q.; Feng, X.; Jin, S. B.; Chen, X.; Ding, X. S.; Jiang, D. L. Pore Surface Engineering in Covalent Organic Frameworks, Nat. Commun. 2011, 2, 536.


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(18) Aiyappa, H. B.; Thote, J.; Shinde, D. B.; Banerjee, R.; Kurungot, S. Cobalt-Modified Covalent Organic Framework as a Robust Water Oxidation Electrocatalyst, Chem. Mater. 2016, 28, 4375−4379. (19) Jiang, H. L.; Akita, T.; Ishida, T.; Haruta, M.; Xu, Q. Synergistic Catalysis of Au@Ag Core−Shell Nanoparticles Stabilized on Metal−Organic Framework, J. Am. Chem. Soc. 2011, 133, 1304−1306. (20) Chan-Thaw, C. E.; Villa, A.; Katekomol, P.; Su, D. S.; Thomas, A.; Prati, L. Covalent Triazine Framework as Catalytic Support for Liquid Phase Reaction, Nano Lett. 2010, 10, 537−541. (21) Pachfule, P.; Panda, M. K.; Kandambeth, S.; Shivaprasad, S. M.; Díazc, D. D.; Banerjee, R. Multifunctional and Robust Covalent Organic Framework–Nanoparticle Hybrids, J. Mater. Chem. A. 2014, 2, 7944−7952. (22) Wan, S.; Andara, F. G.; Asano, A.; Furukawa, H.; Saeki, A.; Dey, S. K.; Liao,

L.;

Ambrogio, M. W.; Botros, Y. Y.; Duan, X. F.; Seki, S.; Stoddart, J. F.; Yaghi, O.M.. Covalent Organic Frameworks with High Charge Carrier Mobility, Chem. Mater. 2011, 23, 4094–4097. (23) Chen, L.; Furukawa, K.; Gao, J.; Nagai, A.; Nakamura, T.; Dong, Y. P.; Jiang, D. L.. Photoelectric Covalent Organic Frameworks: Converting Open Lattices Into Ordered Donor– Acceptor Heterojunctions, J. Am. Chem. Soc. 2014, 136, 9806–9809. (24) Stephenson, N. A.; Bell, A. T.. Mechanistic Insights Into Iron Porphyrin-Catalyzed Olefin Epoxidation by Hydrogen Peroxide: Factors Controlling Activity and Selectivity, J. Mol. Catal. A: Chem. 2007, 275, 54–62.


19


Page 20 of 24

(25) Morris, W.; Volosskiy, B.; Demir, S.; Gándara, F.; McGrier, P. L.; Furukawa, H.; Cascio, D.; Stoddart, J. F.; Yaghi, O. M. Synthesis, Structure, and Metalation of Two New Highly Porous Zirconium Metal–Organic Frameworks, Inorg. Chem. 2012, 51, 6443–6445. (26) Dong, Y. M.; Zhang, J. J.; Jiang, P. P.; Wang, G. L.; Wu, X. M.; Zhao, H.; Zhang, C. Superior Peroxidase Mimetic Activity of Carbon Dots–Pt Nanocomposites Relies on Synergistic Effects, New J. Chem. 2015, 39, 414–416. (27) Gao, L. Z.; Zhuang, J.; Nie, L.; Zhang, J. B.; Zhang, Y.; Gu, N.; Wang, T. H.; Feng, J.; Yang, D. L.; Perrett, S.; Yan, X. Y. Analytical and Advanced Methods-Based Determination of Melamine in Food Products, Nat. Nanotechnol. 2007, 2, 577–583. (28) Chen, G. X.; Zhao, Y. ; Fu, G.; Duchesne, P. N.; Gu, L.; Zheng, Y. P.; Weng, X. F.; Chen, M. S.; Zhang, P.; Pao, C. W.; Lee, J. F.; Zheng, N. F. Interfacial Effects in Iron-Nickel Hydroxide–Platinum Nanoparticles Enhance Catalytic Oxidation, Science. 2014, 344, 495–499. (29) Liu, W. G.; Zhang, L. L.; Liu, X.; Liu, X. Y.; Yang, X. F.; Miao, S.; Wang, W. T.; Wang, A.Q.; Zhang, T. Discriminating Catalytically Active FeNx Species of Atomically Dispersed Fe− N−C Catalyst for Selective Oxidation of the C−H Bond, J. Am. Chem. Soc. 2017, 139, 10790– 10798. (30) De Smit, E.; Van Schooneveld, M. M.; Cinquini, F.; Bluhm, H.; Sautet, P.; De Groot, F. M.; Weckhuysen, B. M. On the Surface Chemistry of Iron Oxides in Reactive Gas Atmospheres. Angew. Chem. Int. Ed. 2011, 50, 1584–1588. (31) Zhou, D.; Cao, X. Q.; Wang, Z; Hao, S. A.; Hou, X. D.; Qu, F. L.; Du, G.; Asiri, A. M.; Zheng, C. B.; and Sun, X. P. Fe3N-Co2N Nanowires Array: A Non-Noble-Metal Bifunctional


20

Page 21 of 24 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


Catalyst Electrode for High-Performance Glucose Oxidation and H2O2 Reduction toward NonEnzymatic Sensing Applications. Chem. Eur. J. 2017, 23, 5214–5218. (32) Hsiao, C. L.; Chou, I. C.; Okafor, C. D.; Bowman, J. C.; O’Neill, E. B.; Athavale, S. S.; Petrov, A. S.; Hud, N. V.; Wartell, R. M.; Harvey, S. C.; Williams, L. D. RNA with Iron (II) as a Cofactor Catalyses Electron Transfer. Nat. Chem. 2013, 5, 525−528. (33) Zhang, L. B.; Guo, S. J.; Zhu, J. B.; Zhou, Z. X.; Li, T.; Li, J.; Dong, S. J.; Wang, E. K. Engineering DNA Three-Way Junction with Multifunctional Moieties: Sensing Platform for Bioanalysis. Anal. Chem. 2015, 87, 11295−11300. (34) Zhao, H.; Dong, Y. M.; Jiang, P. P.; Wang, G. L.; Zhang, J. J. Highly Dispersed CeO2 on TiO2 Nanotube: A Synergistic Nano-composite with Superior Peroxidase-Like Activity. ACS Appl. Mater. Interfaces. 2015, 7, 6451.6461. (35) Li, B. L.; Du, Y.; Li, T.; Dong, S. J. Investigation of 3,3′,5,5′-tetramethylbenzidine as Colorimetric Substrate for a Peroxidatic DNAzyme, Anal. Chim. Acta. 2009, 651, 234–240. (36) Adhikamsetty, R. k.; Gollapalli, N. R.; Jonnalagadda, S. B. Complexation Kinetics of Fe2+ with 1, 10-phenanthroline Forming Ferroin in Acidic Solutions, Int. J. Chem. Kinet. 2008, 40, 515–523. (37) André, R.; Natálio, F.; Humanes, M.; Leppin, J.; Heinze, K.; Wever, R.; Schröder, H. C.; Müller, W .E. G.; Tremel, W. V2O5 Nanowires with an Intrinsic Peroxidase-Like Activity, Adv. Funct. Mater. 2011, 21, 501–509.


21


Page 22 of 24

(38) He, W. W.; Wu, X. C.; Liu, J. B.; Hu, X. N.; Zhang, K.; Hou, S. A.; Zhou, W. Y.; Xie, S. S. Design of AgM Bimetallic Alloy Nanostructures (M = Au, Pd, Pt) with Tunable Morphology and Peroxidase-Like Activity, Chem. Mater. 2010, 22, 2988–2994. (39) Dutta, A. K.; Maji, S. K.; Srivastava, D. N.; Mondal, A.; Biswas, P.; Paul, P.; Adhikary, B. Synthesis of FeS and FeSe Nanoparticles from a Single Source Precursor: a Study of Their Photocatalytic Activity, Peroxidase-Like Behavior, and Electrochemical Sensing of H2O2, ACS Appl. Mater. Interfaces. 2012, 4, 1919–1927. (40) Tan, H. L.; Ma, C. J.; Gao, L.; Li, Q.; Song, Y. H.; Xu, F. G.; Wang, T.; Wang, L. MetalOrganic Framework-Derived Copper Nanoparticle@Carbon Nanocomposites as Peroxidase Mimics for Colorimetric Sensing of Ascorbic Acid, Chem. Eur. J. 2014, 20, 16377–16383. (41) Ishibashi, K.; Fujishima, A.; Watanabe, T.; Hashimoto, K. Quantum Yields of Active Oxidative Species Formed on TiO2 Photocatalyst, J. Photochem. Photobiol. A. 2000, 134, 139– 142. (42) Qian, X. F.; Ren, M.; Fang, M.Y.; Kan, M.; Yue, D. T.; Bian, Z. F.; Li, H. X.; Jia, J. P.; Zhao,Y. X. Hydrophilic mesoporous carbon as iron(III)/(II) electron shuttle for visible light enhanced Fenton-like degradation of organic pollutants, Appl. Catal. B: Environ. 2018, 231, 108–114. (43) Chen, Y. J.; Cao, H. Y.; Shi, W. B.; Liu, H.; Huang, Y. M. Fe–Co Bimetallic Alloy Nanoparticles as a Highly Active Peroxidase Mimetic and its Application in Biosensing, Chem. Commun. 2013, 49, 5013–5015.


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(44) Sun, J. Y.; Ge, J. C.; Liu, W. M.; Lan, M. H.; Zhang, H. Y.; Wang, P. F.; Wang, Y. M.; Niu, Z. W. Multi-Enzyme Co-Embedded Organic-Inorganic Hybrid Nanoflowers: Synthesisand Application as a Colorimetric Sensor, Nanoscale. 2014, 6, 255–262. (45) Li, R. M.; Zhen, M. M.; Guan, M. R.; Chen, D. Q.; Zhang, G. Q.; Ge, J. C.; Gong, P.; Wang, C. R.; Shu, C. Y. A Novel Glucose Colorimetric Sensor Based On Intrinsic PeroxidaseLike Activity of C60-Carboxyfullerenes. Biosens. Bioelectron. 2013, 47, 502–507.


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