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A Journal of
Accepted Article
Title: Stereoselective nanozyme based on ceria nanoparticles
engineered with amino acids
Authors: Xiaogang Qu, Yuhuan Sun, Chuanqi Zhao, Nan Gao, and
Jinsong Ren
This manuscript has been accepted after peer review and appears as an
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of the final Version of Record (VoR). This work is currently citable by
using the Digital Object Identifier (DOI) given below. The VoR will be
published online in Early View as soon as possible and may be different
to this Accepted Article as a result of editing. Readers should obtain
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content of this Accepted Article.
To be cited as: Chem. Eur. J. 10.1002/chem.201704579
Link to VoR:
Supported by
Chemistry - A European Journal
Stereoselective nanozyme based on ceria nanoparticles
engineered with amino acids
Abstract: Stereoselectivity towards substrate is one of the most
important characteristics of enzymes. Amino acids, as cofactors of
many enzymes, play important roles in stereochemistry. Herein,
chiral nanozymes were constructed by grafting a series of D- or Lamino acids on surfaces of ceria (cerium oxide) nanoparticles. We
selected the most commonly used drug for combating Parkinson?s
disease 3, 4-dihydroxyphenylalanine (DOPA) enantiomers as
examples for chiral catalysis. Through detailed kinetic studies of
eight amino acids modified cerium oxide nanoparticles (CeNP), we
found that phenylalanine-modified CeNP was optimal for the DOPA
oxidation reaction and showed excellent stereoselectivity towards its
enantiomers. L-phenylalanine-modified CeNP showed higher
catalytic ability for oxidation of D-DOPA while D-phenylalaninemodified CeNP were more effective to L-DOPA. Taken together, the
results indicated that stereoselective nanozyme can be constructed
by grafting nanozyme with chiral molecules. This work may inspire
better design of chiral nanozymes.
Chirality is one of the most important characteristics of living
system. Biomolecules, such as amino acids, sugars, DNA and
protein are chiral. Living systems are very sensitive to the chiral
species, such as drugs, because the interaction between two
chiral species is usually in an enantiospecific way.1 Increasing
researches showed that the chiral selectivity is one of life?s
distinctive biochemical signatures, is a prerequisite in many
biological processes.2
Natural enzymes are innately chiral and always consist of Lamino acids (with the exception of glycine). Their catalytic
activity is highly dependent on the steric configuration of
substrate.3 For instance, natural nucleases can only cleave the
phosphodiester bonds of natural DNA substrate. However, LDNA, as the enantiomer of natural DNA, cannot be digested by
nucleases because of their nonnative chirality.4 Although bearing
high catalytic activity and specificity, natural enzymes possesses
some shortcomings, such as low stability, difficulty in preparation,
sensitivity to environmental conditions.5 Recently, remarkable
progress has been made in developing artificial enzyme,
especially nanomaterial-based artificial enzymes (nanozymes),
which have been widely applied in biosensing, immunoassays,
Y. Sun, Dr. C. Zhao, Dr. N. Gao, Prof. J. Ren and Prof. X. Qu
Laboratory of Chemical Biology and State Key Laboratory of Rare
Earth Resource Utilization,
Changchun Institute of Applied Chemistry, Chinese Academy of
Changchun, Jilin 130022, China.
Y. Sun
University of Science and Technology of China,
Hefei, Anhui 230026, China
Supporting information containing the experimental section and
additional characterization is available from the Wiley Online Library
or from the author
cancer diagnostics and therapy, etc.6 In the field of nanozymes,
most attention has been paid to improve enzymatic activity, 7
realize new catalytic reactions, construct novel multi-nanozymes
and exploit their applications. However, few investigations
involve the chiral selectivity of nanozymes.
Various nanomaterials have been used as nanozymes to
mimic natural enzymes. Metal oxide nanoparticles are of
particular interests because of both their acid?base and redox
properties.8 Cerium oxide nanoparticles (CeNP), is one of the
most widely used metal oxide catalysts.9 CeNP have been
reported to have multienzyme mimetic activity, including
superoxide oxidase (SOD), catalase and oxidase. 10 This is
probably related to the coexistence of both Ce3+ and Ce4+ on the
surface, where the Ce3+ species is coupled with oxygen
vacancies. In addition, the properties of CeNP could be
controlled and tailored in predictable synthetic methods to satisfy
requirements of specific functions.11 Perez and colleagues
prepared CeNP with oxidase-like activity to achieve colorimetric
or fluorigenic immunoassays.12 However, they did not refer to
the chiral selectivity, which is the indigenous property of enzyme.
In order to better imitate the natural enzymes, stereoselectivity
would be an unnegligible factor.
Scheme 1. Illustration of stereoselective catalytic oxidation of the DOPA
enantiomers by the phenylalanine-modified CeNP. With the catalysis of
CeNP@D-Phe, L-DOPA was oxidized more effecively into L-dopachrome.
Conversely, D-DOPA was oxidized more effectively than L-DOPA with
Herein, we found that 3, 4-dihydroxyphenylalanine (DOPA), as
the most commonly used drug for combating Parkinson?s
disease,13 can be catalytically oxidized by CeNP. Then, we set
This article is protected by copyright. All rights reserved.
Accepted Manuscript
Yuhuan Sun,[a,b] Chuanqi Zhao,[a] Nan Gao,[a] Jinsong Ren,[a] and Xiaogang Qu*[a]
Chemistry - A European Journal
out to construct chiral artificial oxidase by using D- or L-amino
acids as the coating agents to confer the stereoselective
property on the CeNP (Scheme 1). Amino acids can be
cofactors of natural enzymes, and the stereochemical relation
between amino acids and substrates plays important roles.14 For
a comprehensive understanding, D- or L-amino acids were used
for our study, including nonpolar amino acids (phenylalanine
(Phe), alanine (Ala) and tryptophan (Trp)), and polar amino
acids (histidine (His), glutamic acid (Glu), arginine (Arg), lysine
(Lys) and tyrosine (Tyr)). Among these kinds of amino acidmodified cerium nanoparticles (CeNP@AA) we studied,
phenylalanine-modified cerium nanoparticles (CeNP@Phe)
showed optimal enzymatic activity. More importantly,
CeNP@Phe exhibited excellent stereoselectivity for DOPA
enantiomers as well. CeNP@L-Phe showed higher catalytic
ability for D-DOPA while CeNP@D-Phe were more effective to
L-DOPA. The D- and L- stereoselectivity has been further
studied and verified.
Firstly, various amino acids-modified CeNP with oxidase-like
activity were fabricated. Poly (acrylic acid)-coated CeNP were
synthesized by an in situ procedure for the following modification.
Transmission electron microscopy (TEM) images revealed the
particle diameter about 4.3 nm with well uniform distribution
(Figure 1A and Figure S1). Due to their small size, CeNP
exhibited high surface to volume ratio which would profoundly
benefit their enzymatic activity. CeNP were further examined by
X-ray photoelectron spectroscopy (XPS) to determine the mixed
oxidation states (Figure 1B).15 Next, various amino acids were
respectively modified onto the surface of CeNP via an amidation
approach. The Fourier transform infrared (FT-IR) spectroscopy
showed an obvious vibration band around 1656 cm?1, which
confirmed the formation of acylamide bonds (Figure 1C). The
corresponding thermo gravimetric analysis (TGA) plot
demonstrated the coverage of amino acids was comparable
Figure 1. Materials characterization of cerium oxide-based nanoparticles. (A)
TEM image of CeNP. The inset is magnification of one segment. (B) XPS
analysis of CeNP. (C) FT-IR spectra of CeNP and its derivatives. (D) XRD
patterns of CeNP and CeNP@Phe.
(Figure S2). Powder X-ray diffraction (XRD) patterns of
CeNP@AA matched exactly to that of CeNP (Figure 1D),
supporting the unspoiled crystal structure.
We next evaluated the oxidase-like activity of the CeNP
towards DOPA. As promising candidates, CeNP could catalytic
oxidation of various organic substrates including 3, 3?, 5, 5?tetramethylbenzidine
(3ethylbenzothizoline-6-sulfonic acid) (ABTS) and dopamine.12a
Based on UV-vis absorption measurements, the oxidation of
DOPA was proved by the appearance of absorbance at 475
nm.16 Simultaneously, the obvious colour change from
colourless to brown also demonstrated the oxidation of DOPA
(Figure 2A). These experiments confirmed that CeNP could
catalyze the oxidation of DOPA to dopachrome. It should be
noted that CeNP acted as multivalent or cooperative catalysts,
which was confirmed by the departure from linearity between
initial rates versus concentration of CeNP (Figure S3).17
As shown in Figure 2B, after modified with amino acids, CeNP
decreased the catalytic activity for DOPA to some extent. These
results were understandable because some active sites of CeNP
have been shielded by amino acids. Subsequently, we
attempted to screen the optimal amino acids for constructing the
stereoselective nanozyme through DOPA oxidation. Nonpolar
amino acids (Phe with aromatic side chain, Ala with alkyl side
chain), and polar amino acids (His with alkaline side chain, Glu
with acid side chain) were modified respectively onto the surface
of CeNP at first. By monitoring the absorbance change at 475
nm, the catalytic oxidation of DOPA by each of CeNP@AA was
Figure 2. (A) UV/Vis spectra of CeNP (black line) and the oxidation of LDOPA in the absence (red line) and presence (blue line) of CeNP. The
spectrum was monitored after 2 min. The inset shows the color change of
CeNP after adding DOPA. (B) Saturation curves corresponding to the
oxidation rate of DOPA to dopachrome at variable concentrations of D-DOPA,
in the absence and presence of CeNP, CeNP@Phe, CeNP@His, CeNP@Ala,
CeNP@Glu, respectively. The concentration of nanoparticles was 15 ?g/mL.
The error bars represented the standard deviation of three measurements. (C)
Schematic representation of different active energies of DOPA oxidation with
various CeNP@AA. (D) The integration trends of Vmax and Ea of DOPA
oxidation with CeNP@AA. Ea was in black line and boxes. Vmax was in red line
and circles.
This article is protected by copyright. All rights reserved.
Accepted Manuscript
Chemistry - A European Journal
examined (Figure S4). We observed that all CeNP@AA showed
typical saturation kinetics (Figure 2B). Corresponding data were
analysed in terms of the Michaelis?Menten model (Figure S4F
and Table S2). Clearly, the different CeNP@AA differed in their
catalytic performance. Among them, phenylalanine-modified
cerium oxide nanoparticles (CeNP@Phe) revealed the highest
catalytic efficiency towards DOPA. CeNP@His were also found
to have a high catalytic activity. Yet CeNP@Glu showed the
lowest catalytic performance. We inferred that the aromatic
property (ie. Phe, His) and positively charged property (ie. His)
of amino acids may be important factors for the high catalytic
activity of CeNP@AA. We next investigated CeNP modified with
several other amino acids, including tyrosine and tryptophan
(aromatic amino acids), arginine and lysine (positively charged
amino acids), to further optimize appropriate amino acids for the
oxidation of DOPA (Figure S5). Clearly, aromatic amino acids
modified CeNP had relatively higher catalytic activity and
CeNP@Phe had the fastest catalytic rate. Next, On the basis of
Arrhenius equation,18 the active energies of DOPA oxidation by
various CeNP@AA were estimated (Figure 2C and Figure S6).
Obviously, among them, CeNP@Phe had the lowest activation
energy, which was in good agreement with its highest catalytic
activity. To sum up the kinetic analyses (Figure 2D), CeNP@AA
enabled function as a nanozyme, and CeNP@Phe were optimal
for the oxidation reaction of DOPA.
chiroselective performance of CeNP conjugated with
phenylalanine enantiomers were examined, respectively (Figure
S8). Based on Michaelis?Menten model, we analyzed and
compared the kinetic parameters, which were summarized in
Table 1. The Michaelis?Menten constant (Km) was estimated by
Lineweaver?Burk plots (Figure S9). The smaller Km, the higher
binding affinity between enzymes and substrates. 19 Catalytic
number (Kcat) indicates the ability of enzyme to catalyze one
certain substrate.20 Kcat/Km is usually applied for describing the
catalytic efficiency of one enzyme.21 With regard to CeNP@DPhe (Figure 3C), Kcat for L- and D-DOPA were 3.12�?3 s?1,
and 1.94�?3 s?1 (Table 1), respectively, indicating the higher
catalytic ability of CeNP@D-Phe for oxidizing L-DOPA than DDOPA. Moreover, a lower Km value was observed for L-DOPA
than D-DOPA, implying the stronger binding affinity of
CeNP@D-Phe for L-DOPA. In addition, Kcat/Km of CeNP@D-Phe
was higher for L-DOPA than D-DOPA, implying that CeNP@DPhe had higher catalytic efficiency (1.87 fold difference) for LDOPA than D-DOPA. These results would be discussed in detail
in the following section. Accordingly, as contrast, the catalytic
efficiency of CeNP@L-Phe for DOPA enantiomers was also
studied and just a 1.13 fold difference was observed (Figure 3D
and Table 1), indicating that, compared with CeNP@D-Phe,
CeNP@L-Phe exhibited a weaker stereoselectivity for DOPA
enantiomers. Beside CeNP@D-Phe, CeNP@D-His was also
found to have obvious stereoselectivity. However, the trend of
stereoselectivity was different from that with CeNP@D-Phe.
CeNP@D-His exhibited higher catalytic ability for D-DOPA.
(Figure S10 and Table S3). On the basis of the above results,
modification of amino acids endowed nanoceria with
stereoselectivity and its stereoselectivity was related to the
chirality of the amino acid.
Table 1. Kinetic Parameters for catalytic oxidation of DOPA enantiomers by
CeNP@D-Phe and CeNP@L-Phe.
Nanoenzyme [a]
Figure 3. (A) The time-dependent absorbance changes of DOPA at 475 nm in
the absence or presence of CeNP. (B) The absorbance change of DOPA
enantiomers with CeNP@L-Phe, CeNP@D-Phe at 100s intervals. Saturation
curves for the enantiomers of DOPA catalytic oxidation by CeNP@D-Phe (C),
CeNP@L-Phe (D). All reactions were carried out in citric acid (25 mM) buffer,
45 癈. Error bars represent standard deviations of measurements (n = 3).
Subsequently, we discussed the catalytically stereoselectivity
of CeNP@AA towards DOPA enantiomers. The unmodified
CeNP did not show any chiral selectivity for oxidation of L- and
D-DOPA (Figure 3A), implying that the unmodificated nanozyme
did not hold stereoselectivity. Howbeit the modification of amino
acids could lead the difference for the oxidation of DOPA
enantiomers (Figure S7). Therein, CeNP@Phe displayed
relatively high stereoselective (Figure 3B). Thus, the catalytic
Kcat (10-3
(10-3 s-1
[a] The concentration of nanozymes was calculated on the basis of the total
mass of the Ce metal. The Ce content in these mimetic enzymes was
determined by ICP analysis (see Table S1). [b] Selectivity factor of
CeNP@L-Phe equals [Kcat/Km]D-DOPA/[Kcat/Km]L-DOPA. Selectivity factor of
CeNP@D-Phe equals [Kcat/Km]L-DOPA/[Kcat/Km]D-DOPA. Each standard deviation
was calculated from three measurements.
For further understanding the different stereoselectivity, the
molecular docking between different amino acids and DOPA
was carried out with Discovery Studio 2.0 using CDdock
protocol.22 As shown in Figure 4, both DOPA enantiomers can
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Accepted Manuscript
Chemistry - A European Journal
towards oxidation of L-DOPA than that of D-DOPA. In contrast,
CeNP@L-Phe had higher oxidation ability for D-DOPA. Our
results indicated that stereoselective nanozyme can be
constructed by grafting nanozyme with chiral molecules. This
work may inspire better design of chiral nanozymes. To this
end, for example, peptide, nucleic acids and saccharide are
This work was supported by the 973 Project (2012CB720602),
and NSFC (21210002, 21431007, 21533008, 21572216).
Keywords: stereoselectivity ? nanozymes ? ceria nanoparticles ?
amino acids ? DOPA
Figure 4. Energy-minimized average interaction models of (A) D-Phe with LDOPA, (B) D-Phe with D-DOPA, (C) L-Phe with D-DOPA and (D) L-Phe with
L-DOPA. These complexes were shown in ball-and-stick model. Carbon
atoms were indicated in black balls, hydrogen atoms were in gray, oxygen
atoms were in red, while blue balls defineed nitrogen atoms. ?-? aromatic
packing interaction was shown by a henna dash, and hydrogen bonds were
shown by green dashes.
In summary, we successfully prepared a stereoselective
artificial oxidase based on CeNP and chiral amino acids. The
active centre of this nanozyme is CeNP, while amino acids act
as chiral recognition sites for DOPA. Among eight amino acids
we studied, CeNP@D-Phe showed higher catalytic activity
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This article is protected by copyright. All rights reserved.
Accepted Manuscript
interact with phenylalanine enantiomers and form hydrogen
bonding. For the interaction between L-DOPA and D-Phe,
three hydrogen bonds were formed. More importantly, ?-?
aromatic packing interaction was further enhanced the
interactions. These revealed that L-DOPA interacted strongly
with D-Phe, which was in good accordance with our results
that CeNP@D-Phe had the highest catalytic activity for LDOPA. In addition, molecular docking between histidine and
DOPA enantiomers was also conducted (Figure S11). The
results results showed that L-DOPA had stronger binding
affinity with L-His, which was consistent with the
stereoselectivity of CeNP@L-His for L-DOPA. This further
indicated that the chirality of amino acids greatly influenced the
stereoselectivity. It was worth noting that stereoselectivity of
CeNP@His enantiomers were opposite to that of the
CeNP@Phe enantiomers. This difference was still due to the
different interactions between D- or L-amino acid and D- or LDOPA. It also inferred that the stereoselectivity of CeNP@AA
was not just following amino acid?s chirality, it concerned with
many factors. Although more detailed mechanism of amino
acids?DOPA interaction on CeNP deserves further studies,
this is the first time to show that nanoceria as a nanozyme with
stereoselectivity, our results clearly indicated that chiral
recognition between amino acids and DOPA played a vital role
in the stereoselective catalysis.
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This article is protected by copyright. All rights reserved.
Accepted Manuscript
Chemistry - A European Journal
Yuhuan Sun, Chuanqi Zhao, Nan Gao,
Jinsong Ren and Xiaogang Qu*
Page No. ? Page No.
Stereoselective nanozyme based on
ceria nanoparticles engineered with
amino acids
Accepted Manuscript
Stereoselective artificial oxidase is
constructed by grafting chiral amino
acids on surfaces of cerium oxide
nanoparticles. Among eight kinds of
amino acids we studied,
phenylalanine-modified CeNP is
optimal for the DOPA oxidation
reaction and show excellent
stereoselectivity towards its
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