Biosensors and Bioelectronics
Biosensors and Bioelectronics
Biosensors and Bioelectronics
A R T I C L E I N F O A BS T RAC T
Keywords: We herein describe novel amine-grafted metal–organic frameworks (MOFs) as a promising alternative to
Metal–organic framework natural peroxidase enzyme and their applications for a fluorescent assay of choline (Cho) and acetylcholine
Amine grafting (ACh). Among diverse amine-functionalized MOFs, N,N,N′,N′-tetramethyl-1,4-butanediamine (TMBDA)-
Peroxidase-like activity functionalized MIL-100(Fe) (TMBDA-MIL-100(Fe)) exhibited the highest peroxidase activity by developing
Choline detection
intense fluorescence from Amplex UltraRed (AUR) in the presence of H2O2, which was presumably due to the
Acetylcholine detection
synergetic effect of the enhanced negative potential and precisely controlled molecular size of the grafted
diamine. Based on the excellent peroxidase-like activity of TMBDA-MIL-100(Fe), choline and ACh were reliably
determined down to 0.027 and 0.036 µM, respectively. Furthermore, practical applicability of this strategy was
successfully demonstrated by detecting choline and ACh in spiked samples of milk and serum, respectively. This
work highlights the advantages of amine-grafted MOFs for the preparation of biomimetic catalysts, extending
their scope to biosensor applications.
⁎
Corresponding author at: Research Group of Nanocatalysts, Korea Research Institute of Chemical Technology (KRICT), Daejeon 34114, Republic of Korea.
⁎⁎
Corresponding author.
E-mail addresses: [email protected] (H.G. Park), [email protected] (Y.K. Hwang).
1
These authors contributed equally to this work.
http://dx.doi.org/10.1016/j.bios.2017.08.056
Received 29 April 2017; Received in revised form 21 August 2017; Accepted 25 August 2017
Available online 30 August 2017
0956-5663/ © 2017 Elsevier B.V. All rights reserved.
A.H. Valekar et al. Biosensors and Bioelectronics 100 (2018) 161–168
new generation of peroxidase-mimicking nanomaterials obtainable by Amine grafting on CUS of MIL-100(Fe) and their characterizations has
simple preparation procedures, with high catalytic activity as well as been described in details in experimental part of the Supporting
excellent stability, is still a hot topic. information.
Recently, biosensors based on enzyme-mimicking organic-inorganic
hybrid nanomaterials such as protein or DNA-Cu nanoflowers (Batule 2.2. Peroxidase-like activity of MOFs with AUR and TMB substrates
et al., 2015; Park et al., 2017), Fe-aminoclay (Lee et al., 2013), and
MOFs (Ai et al., 2013; Dong et al., 2015; Feng et al., 2012; Liu et al., The peroxidase-like activity of the different MOFs was measured in
2013; Qin et al., 2013; Zhang et al., 2014) have been successfully a 50 µL reaction solution containing H2O2 (1 mM), MOF (0.2 mg/mL),
exploited. Among these, MOFs have emerged as a new class of crystalline and 3,3′,5,5′-tetramethylbenzidine (TMB) (1 mM) or AUR (50 µM) as
hybrid porous materials by taking advantages of their intriguing colorimetric or fluorogenic substrate, respectively, in Tris acetate buffer
structural properties such as high specific surface area, tunable pore (5 mM, pH 7) on the basis of the absorbance recorded at 500–700 nm
size distribution, coordinatively unsaturated metal sites (CUS) in the (maximum at 650 nm) and fluorescence at Ex-540 nm and Em-570–
skeleton, and practically limitless choice of metals and organic ligands 650 nm (maximum at 588 nm). The fluorescence intensities were
affording an essentially infinite number of possible combinations. These measured using a Tecan Infinite M200 pro microplate reader
fascinating features led them to be widely used in many fields, such as (Mannedorf, Switzerland) with black, 384-well Greinier Bio-one micro-
gas storage (Llewellyn et al., 2008; Murray et al., 2009), gas separation plates (ref: 781077, Courtaboeuf, France).
(Li et al., 2012; Wuttke et al., 2012), catalysis (Horcajada et al., 2007;
Lee et al., 2009; Valekar et al., 2016), and sensing (Desai et al., 2015; 2.3. Quantification of choline and acetylcholine
Kumar et al., 2015; Meilikhov et al., 2013; Nagarkar et al., 2013).
Besides their aforementioned unique properties, MOFs provide great Detailed description on quantification of choline and acetylcholine
potential for the further functionalization of their structures. According can be found in supporting information of the manuscript.
to the literature, post synthetic modification (PSM, where one can do the
modification in original MOF structure after its synthesis) is considered 3. Results and discussion
as the most common method to achieve the desired functionality in
MOFs, subsequently, anticipated chemical and physical property can be 3.1. Amine grafting on CUS of MIL-100(Fe)
imparted (Tanabe and Cohen, 2011). Therefore, a large number of
functional MOFs have been prepared using the PSM and successfully The present biosensor system for fluorescent quantification of Cho
utilized to improve their performance in catalysis (Banerjee et al., 2009; and ACh consists of acetylcholine esterase (AChE) and choline oxidase
Hwang et al., 2008; Kasinathan et al., 2011) and gas storage (Dinca (ChOx), which would generate H2O2 by their consecutive catalytic
et al., 2007; Wang and Cohen, 2009). However, functionalized MOFs oxidation from acetylcholine. This would activate amine-functionalized
containing redox-active metal centers have rarely been used as perox- MOF to convert selected substrate, AUR, into highly fluorogenic
idase mimics mainly due to their hydrothermal and chemical instability product (oxAUR) (Fig. 1a). For the development of functional MOFs
(Larsen et al., 2011; Qin et al., 2013). with enhanced peroxidase-like activity, the post-synthetic amine func-
The previous reported MOF biosensors are simply used either as tionalization was carried out by grafting of diamines on the CUS of
synthesized Fe based MOFs such as MIL-53, MIL-68, MIL-88-NH2, MIL-100(Fe), as illustrated in Fig. 1b. The diamine compounds used
MIL-100, and MIL-101, or Hemin@MIL-101(Al)-NH2 composite for for the functionalization include ethylene diamine (ED), N,N′-di-
peroxidase mimics (Ai et al., 2013; Dong et al., 2015; Feng et al., 2012; methyl-1,3-propanediamine (DMPDA), and N,N,N′,N′-tetramethyl-
Liu et al., 2013; Qin et al., 2013; Zhang et al., 2014). However, these 1,4-butanediamine (TMBDA).
studies did not utilize one of the most promising approaches of The stability of the amine modified MIL-100(Fe) frameworks was
functionalizing MOF on CUS with desired functionality. In this work, investigated using X-ray powder diffraction analysis (XRPD) (Fig. 2a).
we took this opportunity for the first time and functionalized MIL- The powder diffraction patterns of the functionalized samples showed
100(Fe) by grafting various aliphatic diamines on its CUS. The decreased peak intensity compared to the pristine MOF. This result is
performance of functionalized MIL-100(Fe) for peroxidase mimic consistent with previous reports showing a reduction in the peak
activity enhanced significantly compared to its pristine form presum-
ably due to the synergetic effect of the enhanced negative potential and
precisely controlled molecular size of the grafted diamines. Based on
this enhanced peroxidase-like activity, we developed a simple and
effective fluorescent method for the quantitative determination of
choline and acetylcholine. These two biomolecules serve as important
regulators in many biological processes including nutrition and neuro-
transmission, however until now, their detection methods have been
suffered from many limitations such as low sensitivity, unstable signal,
and complex experimental steps (Chen et al., 2011). Thus, there is a
significant incentive to develop sensitive, reliable, and convenient assay
of choline and acetylcholine. Herein, we used amine-functionalized
MOFs coupled with enzymes specific for choline and acetylcholine for
the successful detection of choline and acetylcholine even present in
spiked samples of milk and serum, respectively.
2. Experimental section
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A.H. Valekar et al. Biosensors and Bioelectronics 100 (2018) 161–168
a) b)
700
600
3
500
Intensity (a.u.)
2
3 400 3
300
4
2
200
100
1
0
5 10 15 20 25 0.0 0.2 0.4 0.6 0.8 1.0
2θ (degree) Relativepressure (P/P0)
c) d)
N-H -C=O
Absorbance (a.u.)
4
4
3
3
2 2
1
1
4000 3500 3000 2500 2000 390 392 394 396 398 400 402 404
-1
Wavenumber (cm ) Binding energy (eV)
Fig. 2. a) XRPD patterns, b) N2 physisorption at 77 K, and c) FT-IR spectra at 423 K and d) XPS analysis (N1s) of pristine and amine grafted MIL-100(Fe). 1. Pristine MIL-100(Fe),
2.ED-MIL-100(Fe), 3. DMPDA-MIL-100(Fe), and 4. TMBDA-MIL-100(Fe).
intensity due to the incorporation of diamines in the pores of MOFs The amine grafting was further confirmed by Fourier transform
(Hwang et al., 2008; Kasinathan et al., 2011). The textural properties of infrared (FT-IR) spectroscopy. Fig. 2c shows the spectrum of bare
the pristine and amine-functionalized samples are given in Table S1. MIL-100(Fe) compared with those of different amine-grafted MIL-
After amine functionalization, both surface area and pore volume 100(Fe) compounds. Despite the presence of amine moieties in the
decreased due to different diamines that were attached to the pore framework, no major changes in the FT-IR patterns were observed due
surfaces and partially blocked the pores. However, the N2 adsorption to the low levels of amine grafting. However, two amine-grafted
isotherm patterns remained intact after functionalization (Fig. 2b). The samples, ED-MIL-100(Fe) and DMPDA-MIL-100(Fe), showed a small
pore size distribution (PSD) profiles calculated on the basis of the additional absorption band in the region of 3250–3350 cm−1, which
density functional theory (DFT) showed no significant change in the could be attributed to the characteristic N-H stretching vibration mode,
pore size of MIL-100(Fe) after amine grafting (Fig. S1), probably due to as marked in Fig. 2c. The lack of N-H bonds in TMBDA-MIL-100(Fe)
the low amine loading determined from the “N” content (Table S1). The produced no additional peak in this region. The parent MIL-100(Fe)
grafting of diamines onto the CUS of MIL-100(Fe) occurred to a showed an absorption peak at 1739 cm−1 corresponding to the C˭O
reasonably lower extent when compared with the diamine grafting on stretching and indicating the presence of free trimesic acid, which
the CUS of MIL-101(Cr) and MIL-100(Cr), which was previously decreased in intensity and slightly shifted to the lower wavelength of
reported by Hwang et al. (2008) (Kasinathan et al., 2011) and Cabello 1733 cm−1 after modification with primary (ED) and secondary
et al. (2015), respectively. This indicates that a change of the metal (DMPDA) amines. This suggests that these amine groups can probably
center in the framework of MIL-100 (Fe instead of Cr) can affect the form hydrogen bonds with the free trimesic acid. TMBDA-MIL-100(Fe)
chelating reaction of the amines with the metal in MOFs. This assump- did not show any change in the C˭O stretching frequency, which might
tion could be further supported by the electronic configuration of the be due to the absence of N-H bonds in TMBDA available for hydrogen
Fe(III) center present in MIL-100(Fe). The octahedral unit of Fe(III) bonding. In order to show the presence of the amines on the surface of
possesses a high spin state resulting in a large exchange energy of MIL-100(Fe), we performed X-ray photoelectron spectroscopy (XPS)
electrons in the subshell (Horcajada et al., 2007). Nevertheless, it has analysis (Fig. 2d). The N 1 s peak around 397 eV due to the amine
been proved that the anchoring of a small amount (0.02 mmol/g) of “N” groups was observed in all amine-grafted samples and revealed the
containing polymer on the surface of MIL-100(Fe) can considerably occurrence of amine moieties on the surface of the amine-grafted MIL-
affect its magnetic resonance imaging activity for use in theranostic 100(Fe) samples. The presence of surface amine functionalities affected
applications (Zimpel et al., 2016). Thus, these results encouraged us to the surface charge of the MIL-100(Fe) particles, which was evident
continue our work in view of potential biosensing applications. from the zeta potential measured at neutral pH in an aqueous medium
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A.H. Valekar et al. Biosensors and Bioelectronics 100 (2018) 161–168
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A.H. Valekar et al. Biosensors and Bioelectronics 100 (2018) 161–168
concentration in a range of 1–30 µM with a low detection limit of diseases such as neural tube defects, Alzheimer's and fatty liver disease
0.329 µM was obtained, which implies that the TMBDA-MIL-100(Fe) (Biswas and Giri, 2015; Phillips, 2012). Therefore, an effective detec-
catalytic system could be used in analytical systems for the detection of tion method is of utmost importance to monitor an adequate level of
H2O2. This level of sensitivity is sufficient to enable coupling of the choline in the body.
MOF system with any oxidase to create versatile biosensor (Kim et al., Hence, based on the excellent peroxidase-like activity of TMBDA-
2011b; Shin et al., 2017). Moreover, TMBDA-MIL-100(Fe) was shown MIL-100(Fe) for H2O2 detection, we developed a simple fluorescent
to have good recyclability up to five times with a negligible loss of method for the detection of choline. As shown in Eqs. (1) and (2),
catalytic activity (Fig. S6a). This minor loss in activity was presumably choline can be hydrolyzed by choline oxidase to generate H2O2 that can
due to the incomplete recovery of the MOF nanoparticles from the be utilized in the catalytic oxidation of AUR in the presence of TMBDA-
reaction solution by centrifugation after each cycle. The structure of MIL-100(Fe) to produce oxidized AUR. OxAUR generates fluorescence
this MOF remained unchanged after five recycle tests, as confirmed by upon excitation at 588 nm, which can be used to quantify choline.
SEM analysis (Fig. S6b). Choline oxidase
Choline + O2 + H2O ⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯→ betaine + H2O2 (1)
Choline is related to the B vitamins and is involved in brain 3.6. Detection of acetylcholine (ACh) by employing TMBDA-MIL-
development, muscle movement, and body metabolism (Biswas and 100(Fe)
Giri, 2015). Moreover, it is the precursor of acetylcholine, which is an
important neurotransmitter in the peripheral nervous system (Wei Acetylcholine plays a vital role in both peripheral and central
et al., 2014). In spite of being produced in the human body, its dietary nervous systems. It is involved in brain functions such as alertness,
supplementation is required in order to maintain a proper functionality learning, and memory. Patients with neural disorders such as
(Blusztajn, 1998). Accordingly, choline is widely added in food such as Alzheimer's disease (AD), Parkinson disease, schizophrenia, and pro-
milk and dietary supplements (Chen et al., 2011; Phillips, 2012). gressive dementia were found to have decreased ACh levels (Ehrenstein
However, the inadequate level of choline in the body may cause several et al., 1997; He et al., 2014; Ren et al., 2015). In order to treat these
diseases, the quantification of ACh in biological samples such as blood
Table 1 and neuronal cells is of utmost importance.
Comparison of the apparent Michaelis–Menten constant (Km) and maximum reaction Acetylcholinesterase
rate (Vmax) of TMBDA-MIL-100(Fe) and other peroxidase mimics. Acetylcholine ⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯→ Choline + acetic acid (3)
Catalyst Km/mM Vmax/10−8 M S−1 Reference The hydrolysis of ACh can be catalyzed by acetylcholine esterase to
produce choline (Eq. (3)), which subsequently undergoes a catalytic
H2O2 TMB H2O2 TMB process promoted by ChOx to give H2O2 (Eq. (1)); MOFs can utilize
HRP 0.055 0.317 2.43 3.30 (Liu et al., 2013)
this H2O2 for the oxidation of AUR developing a fluorescence intensity
MIL-100(Fe) 0.064 0.424 1.4 2.1 This work (Eq. (2)). To implement this strategy, first the time-dependent kinetics
TMBDA-MIL- 0.028 0.062 23.3 45 This work were determined with and without acetylcholine (Fig. 5a), and there-
100(Fe) after the optimized conditions such as temperature and pH were
MIL-53(Fe) by CE 0.04 1.08 1.86 8.78 (Ai et al., 2013)
determined to be 37 °C and 7 (Fig. 5b and c), respectively. Through
MIL-53(Fe) by MW 0.03 0.28 0.96 4.48 (Dong et al., 2015)
Fe-MIL-88-NH2 0.206 0.284 7.04 10.47 (Liu et al., 2013) the typical reaction, only the target ACh induced a dramatic increase of
the respective fluorescence intensity (Fig. S9), indicating that this
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A.H. Valekar et al. Biosensors and Bioelectronics 100 (2018) 161–168
Fig. 4. Effect of concentration of a) ChOx (U/mL), b) of TMBDA-MIL-100(Fe) (mg/mL). c) Effect of temperature, and (d) pH on catalytic activity of TMBDA-MIL-100(Fe). e) Choline
concentration-dependent change of the fluorescence intensity; the inset shows the linear range between the fluorescence intensity and choline concentration (0.5–10 µM). The
fluorescence intensity is defined as F-F0, where F0 and F are the fluorescence intensities measured at excitation 540 nm and emission at 588 nm in the absence and presence of choline,
respectively. Relative activity (%) was determined by using the ratio of the colorimetric activity to the maximal activity at each graph.
fluorescent assay is highly selective toward the target ACh in the that the developed method is applicable for the detection of acetylcho-
presence of typical interfering molecules even at 10-fold concentra- line in real serum samples.
tions. This high selectivity is mainly due to the high specificity of AChE
and ChOx toward ACh and choline, respectively. Consequently, as 4. Conclusions
shown in Fig. 5d, a linear relationship (R2 = 0.9902) between
fluorescence intensity and acetylcholine concentration in a range of In this study, we successfully synthesized various diamine-grafted
0.1–10 µM with a detection limit of 0.036 µM was obtained. This LOD MIL-100(Fe) and for the first time systematically investigated their
was among the best results when compared with recently reported peroxidase-like activity. The characterization data of the amine-grafted
biosensors used for the detection of acetylcholine (Table S5), confirm- MIL-100(Fe) were well correlated with their peroxidase-mimicking
ing the high sensitivity of our acetylcholine assay arisen from the activity and it was suggested that the improved catalytic activity was
excellent peroxidase-like activity of amine-grafted MIL-100(Fe). due to the enhanced negative potential of the amine-grafted MIL-
Inspired by the high sensitivity of our sensing system for the 100(Fe) and controlled size of the grafted diamine, which helped to
detection of acetylcholine, we endeavored to detect acetylcholine in bring the substrate in close proximity with the active Fe(III) centers
serum (10%) through a standard addition method. The obtained results present on the MOF surface. However, the detection mechanism
(Table S6) are in good agreement with the added acetylcholine, underlying these effects remains to be determined. We further utilized
showing around 97–103% recovery for acetylcholine, and suggesting the highly enhanced peroxidase activity of the amine-grafted MIL-
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A.H. Valekar et al. Biosensors and Bioelectronics 100 (2018) 161–168
Fig. 5. (a) Time-dependent fluorescence intensities (λmax = 588 nm) of reaction mixtures containing W/ and W/O Ach, (b) Effect of temperature, (c) Effect of pH on catalytic activity of
TMBDA-MIL-100(Fe), and (d) ACh concentration-dependent change of the fluorescence intensity; the inset shows the linear range between the fluorescence intensity and ACh
concentration (0.1–10 µM). The fluorescence intensity is defined as F-F0, where F0 and F are the fluorescence intensities measured at excitation 540 nm and emission at 588 nm in the
absence and presence of acetylcholine, respectively. Relative activity (%) was determined by using the ratio of the colorimetric activity to the maximal activity at each graph.
100(Fe) to develop a simple fluorescent assay to detect choline and Asati, A., Santra, S., Kaittanis, C., Nath, S., Perez, J.M., 2009. Angew. Chem. Int Ed. 48
(13), 2308–2312.
acetylcholine with significantly low detection limits (0.027 and Banerjee, M., Das, S., Yoon, M., Choi, H.J., Hyun, M.H., Park, S.M., Seo, G., Kim, K.,
0.036 µM respectively). The present work encouraging the further 2009. J. Am. Chem. Soc. 131 (22), 7524–7525.
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Acknowledgments Bioelectron. 28 (1), 50–55.
Desai, A.V., Samanta, P., Manna, B., Ghosh, S.K., 2015. Chem. Commun. 51 (28),
This work was supported by the R&D Program of the Institutional 6111–6114.
Dinca, M., Han, W.S., Liu, Y., Dailly, A., Brown, C.M., Long, J.R., 2007. Angew. Chem.
Research Program of KRICT (SI1701-02), and by the Next generation
Int Ed. 46 (9), 1419–1422.
carbon upcycling project of Ministry of Science and ICT. JSC is kindly Dong, W., Liu, X., Shi, W., Huang, Y., 2015. RSC Adv. 5 (23), 17451–17457.
grateful to the National Research Council of Science and Technology Ehrenstein, G., Galdzicki, Z., Lange, G.D., 1997. Biophys. J. 73 (3), 1276–1280.
(NST) for financial support (KN16-15). This work was also supported Feng, D.W., Gu, Z.Y., Li, J.R., Jiang, H.L., Wei, Z.W., Zhou, H.C., 2012. Angew. Chem.
Int Ed. 51 (41), 10307–10310.
by the Mid-career Researcher Support Program through the National Filizola, M., Loew, G.H., 2000. J. Am. Chem. Soc. 122 (1), 18–25.
Research Foundation (NRF) funded by the Ministry of Science, ICT & Gao, L.Z., Zhuang, J., Nie, L., Zhang, J.B., Zhang, Y., Gu, N., Wang, T.H., Feng, J., Yang,
Future planning (MSIP) of Korea (No. 2015R1A2A1A01005393). D.L., Perrett, S., Yan, X., 2007. Nat. Nanotechnol. 2 (9), 577–583.
Garcia-Viloca, M., Gao, J., Karplus, M., Truhlar, D.G., 2004. Science 303 (5655),
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Appendix A. Supplementary material He, S.B., Wu, G.W., Deng, H.H., Liu, A.L., Lin, X.H., Xia, X.H., Chen, W., 2014. Biosens.
Bioelectron. 62, 331–336.
Horcajada, P., Surble, S., Serre, C., Hong, D.Y., Seo, Y.K., Chang, J.S., Greneche, J.M.,
Supplementary data associated with this article can be found in the Margiolaki, I., Ferey, G., 2007. Chem. Commun., 2820–2822.
online version at doi:10.1016/j.bios.2017.08.056. Hwang, Y.K., Hong, D.Y., Chang, J.S., Jhung, S.H., Seo, Y.K., Kim, J., Vimont, A., Daturi,
M., Serre, C., Ferey, G., 2008. Angew. Chem. Int Ed. 47 (22), 4144–4148.
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