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Enzyme-Catalyzed Atom Transfer Radical Polymerization

Huiyue Wang , Xin Hu , Yujing Hu , Ning Zhu , Kai Guo

Progress in Chemistry ›› 2022, Vol. 34 ›› Issue (8) : 1796 -1808.

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Progress in Chemistry ›› 2022, Vol. 34 ›› Issue (8) : 1796-1808 DOI: 10.7536/PC211009
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Enzyme-Catalyzed Atom Transfer Radical Polymerization
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Abstract

Atom transfer radical polymerization (ATRP) is an important method for preparing polymers with controllable molecular weight and polydispersity. However, due to the complex oxygen removal steps, metal catalysts residue, and limited monomer scope, it is difficult for ATRP to be widely used in the large-scale preparation of functionalized polymers/copolymers. With the development of enzyme-catalyzed polymerization, radical polymerization has made significant progress in efficient and convenient oxygen removal, expanding monomer scope, and the synthesis of polymers/copolymers with special (nano) structures. This review highlights the structure of enzymes and their catalytic mechanism in enzyme-catalyzed ATRP. Various enzyme/ enzyme mimics catalysis system (including horseradish peroxidase, hemoglobin, heme, laccase, etc.) employed in ATRP are carefully summarized in order. Finally, the opportunities and challenges of enzyme-catalyzed ATRP are discussed for the further development in this field.

Enzyme-Catalyzed Atom Transfer Radical Polymerization

Contents

1 Introduction

2 Horseradish peroxidase(HRP)catalyzed ATRP

3 Hemoglobin catalyzed ATRP

4 Hemin and Enzyme mimic catalyzed ATRP

5 Laccase catalyzed ATRP

6 GOx-HRP cascade catalysis applied as initiator

7 Conclusion and outlook

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Keywords

ATRP / enzyme / catalysis

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Huiyue Wang, Xin Hu, Yujing Hu, Ning Zhu, Kai Guo. Enzyme-Catalyzed Atom Transfer Radical Polymerization. Progress in Chemistry, 2022, 34(8): 1796-1808 DOI:10.7536/PC211009

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1 Introduction

Atom transfer radical polymerization (ATRP) is an important method to prepare polymers with precise topology, molecular weight and dispersity[1⇓⇓⇓⇓~6]. However, due to the toxicity and residue of transition metal catalysts, the polymerization products are difficult to be used in microelectronics, biomedical and other fields[7⇓~9][10]. In recent years, improved ATRP systems have been developed vigorously. A series of new systems, including initiator continuous regeneration catalyst ATRP (ICAR ATRP), electron transfer regeneration catalyst ATRP (ARGET ATRP), zero-valent copper-catalyzed living radical polymerization (SET-LRP/SARA ATRP)), electroregulated ATRP (eATRP) and photo-induced ATRP, have been proposed, which significantly reduce (or even completely avoid) metal residues in products and expand ATRP technology[11,12][13⇓~15][16][17][18][19⇓⇓~22][23,24]. However, some functionalized monomers are still difficult to be polymerized by ATRP, which limits the further application of this method in the field of preparing functional materials[25]. In addition, in the reaction process of ATRP, free radicals/active species are easily affected by oxygen, resulting in polymerization inhibition and quenching reactions, which reduce the efficiency of the polymerization reaction. Conventionally, freeze-pump-thaw and inert gas protection are needed to eliminate the oxygen in the system. This puts forward higher requirements for deaerator equipment and operation, and also limits the application scenarios of ATRP technology. Therefore, it is urgent to develop new ATRP technologies to expand the range of applicable monomers and prepare new functional polymers/copolymers efficiently and conveniently.
As an efficient and specific biocatalyst, enzyme has been widely used in various reactions because of its green, non-toxic, renewable, mild reaction conditions and environmental friendliness[26][27⇓~29]. In addition, enzyme-catalyzed processes show excellent regioselectivity, stereoselectivity and chemoselectivity, and can be catalyzed under mild conditions, which has been widely used in ring-opening polymerization or polycondensation[30][31⇓⇓⇓~35][36⇓⇓~39]. The use of enzymes in reversibly inactivated radical polymerization (RDRP) has emerged in recent years: Qiao et al., Boyer et al., and Anzesheng et al. Have developed enzyme-involved RAFT, which has been widely used in polymerization-induced self-assembly[40][41][42][43,44]. Bruns et al., di Lena et al., and Matyjaszewski et al. Have successively developed new methods for (mimetic) enzyme-catalyzed ATRP, and have made important progress[26][45,46][47]. According to the different kinds of transition metals, ATRP can use Cu (including Cu (0), Cu (I), Cu (II)), Fe (including Fe (0), Fe (II), F (III)), Ru, Ir and other metals as catalysts to control the polymerization through the change of their valence[48⇓~50][51]. Enzymatic catalysis utilizes the structural similarity between the metal center in the metal-protein structure (such as Horseradish Peroxidase (HRP) with iron center, Laccase with coppercenter, Catalase, etc.) And the transition metal catalytic system to activate the initiator/dormant species and initiate the functional monomer for ATRP[52][53][54,55]. Enzyme-catalyzed systems have significant advantages in the preparation of functional polymers/copolymers, especially in the radical (Co) polymerization of monomers that are difficult to polymerize, such as N-vinylimidazole (NVIm), methacrylic acid (MAA), etc., which expands the application of ATRP technology in the preparation of functional polymer materials.
Enzymes also show great advantages in terms of convenient oxygen removal[56]. Matsuda et al. Developed the glucose oxidase (GOx) deoxygenation method, which has been widely used in photoinitiated and thermally initiated radical polymerization and has shown good deoxygenation effect[57][58][59][60,61]. The application of enzyme-catalyzed deoxygenation in ATRP has the advantages of convenient operation and environmental friendliness, and can break through the limitation of anaerobic conditions of ATRP, even in an open environment[62]. In addition, due to the special structure of the metal active center-protein cavity, enzymes as catalysts have also shown great advantages in the construction of biomimetic nanostructured polymers and the selective construction of functionalized surface layers[63⇓~65].
In this paper, the research progress of enzyme-catalyzed atom transfer radical polymerization in recent years is systematically summarized, and the structure and catalytic mechanism of enzymes are described in detail.The suitable monomer, monomer conversion rate, molecular weight and dispersion, advantages and disadvantages of ATRP catalyzed by (simulated) enzymes with different metal active centers (including HRP, hemoglobin, heme with iron as active center and Laccase, Catalase with copper as active center) were systematically summarized and compared. The development of ATRP systems catalyzed by enzymes and enzyme mimics was reviewed. The application scenarios of enzyme-catalyzed ATRP for the preparation of functional materials were listed. Finally, the research status of enzyme catalysis in ATRP was summarized, and its development prospects and challenges were discussed and prospected.
Table 1 summarizes the relevant performance data for ATRP polymerization of vinyl monomers catalyzed by different enzymes.

2 Horseradish peroxidase (HRP)

Horseradish peroxidase (HRP; EC 1.11.1.7) is a kind of peroxidase, which has a high content in plant horseradish, and is a general term for many kinds of isoenzymes in horseradish. It is a glycoprotein composed of a single peptide chain and iron porphyrin, and its active center contains two metals, iron and calcium. HRP has been widely used in the radical polymerization of vinyl monomers and aromatic compounds. Its structure is shown in the figure (Figure 1A), with 308 amino acid residues and iron porphyrin as the prosthetic group. HRP has a size of about 4.6 * 6.7 * 11.7 nm and a molecular mass of about 40 kDa. The optimum pH value for catalysis is about 5, but the pH value is different due to different hydrogen donors.
HRP mainly catalyzes radical polymerization through hydrogen peroxide (H2O2)/β- diketone/peroxidase ternary redox system, and the specific catalytic mechanism is shown in Figure 1b. Fe (Ⅲ) in the ground state of HRP is oxidized to form Compound Ⅰ in the high oxidation state containing Fe (Ⅳ) center. Subsequently, Compound Ⅰ reacts with H+ in the presence of reducing substrate to give another Compound Ⅱ containing a Fe (Ⅳ) center. Both Compound I and Compound II have strong oxidizing properties. When the H2O2 in the system is excessive, HRP will further react with Compound II to form a complex containing Fe (Ⅲ), and O2,CompoundⅢ will spontaneously return to the native ground state of HRP, while O2 will inhibit the polymerization. Therefore, it is very important to control the amount of H2O2 in the polymerization process catalyzed by HRP, but this does not hinder the use of HRP in the catalysis of controlled radical polymerization.
In 2011, di Lena et al. Developed protease-catalyzed ARGET ATRP, and studied the ARGET ATRP process of acrylic acid polyethylene glycol (PEGA) catalyzed by HRP, catalase and laccase[45,46]. Alkyl halides (2-bromopropionitrile (BPN), 2-bromoethyl isobutyrate (EBiB)) were used as initiators in the reaction, and the catalytic effects of the three enzymes were compared. When catalase was used as catalyst and ascorbic acid as reducing agent, the conversion of monomer was more than 90% at 60 ℃ for 8 H, and the molecular weight Mn of the polymer was 8 700 G/mol, which was close to the theoretical value, and the dispersity was -D ≤ 1.70. When the reaction temperature decreases, the monomer conversion also decreases. When HRP is used as catalyst, the monomer conversion can reach more than 96%, and the polymer dispersion -D is less than or equal to 1.60. In order to improve the stability of catalase, some researchers used polyethylene glycol glycidyl ester (PGMA) and bacterial cellulose to immobilize catalase, which further improved its biocompatibility and thermal stability, and expanded its application[55].
In the same year, Bruns et al. Realized ARGET ATRP of N-isopropylacrylamide (NIPAAm, NIPAm, NIPA) with HRP as catalyst, HEBIB as initiator and AscA as reducing agent without any peroxide[67]. The molecular weight Mn of the obtained polymer is 50 000 ~ 220 000 G/mol, and the dispersion degree-D is 1.40 ~ 1.80. The predicted polymerization mechanism is shown in Figure 2. HRP (FeⅢ) with low valence metal iron center catalyzes HEBIB (dormant species) to produce initial free radicals (active species) and form HRP (FeⅣ) with high valence iron active center. The free radicals/active species initiate monomer polymerization, and the concentration of free radicals in the system is regulated by HRP (Fe-Ⅳ). HRP (FeⅣ) was reduced by AscA to HRP (FeⅢ), which participated in the catalytic reaction again. The results showed that the monomer conversion, molecular weight and dispersity could be controlled by adjusting the pH value of the polymerization system and the concentration of the reducing agent AscA. The main disadvantage of this system is that when the molecular weight of the polymer increases with the reaction time, the polymer with high molecular weight can not reach the active center in the enzyme cavity, which hinders the formation of long-chain polymers, resulting in the increase of short-chain polymers and reducing the controllability of polymerization.
Enzymes have a special structure of active metal center-protein cavity, which can be used as a nanoreactor to provide an ideal platform for the preparation of polymer materials with good biocompatibility and safety. Based on this idea, Bruns et al. Successfully realized HRP-catalyzed ATRP, and then tried to encapsulate this enzymatic polymerization in polymer vesicles as nanoreactors.Polymer vesicles filled with hydrophilic polymers were obtained to mimic the cell structure with concentrated cell sap or viscous cytoskeleton, and to obtain nano-aggregates with unique properties[68]. Poly (dimethylsiloxane) -block-poly (2-methyl-2-oxazoline) (PDMS-b-PMOXA) diblock polymer forms nanoaggregates by self-assembly and encapsulates HRP (Figure 1). By adding 2-hydroxy-4 '- (2-hydroxyethoxy) -2-methylpropiophenone (PP-OH) as a photoreactant, a nanovesicle reactor through which small molecular compounds can pass was constructed. Polyethylene glycol acrylate (PEGA) was used as monomer, HEBIB as initiator and sodium ascorbate (NaAsc) as reducing agent. In the reaction process, the monomer, the initiator and the reducing agent of the small molecule are dissolved in the phosphate buffer and enter the vesicle reactor for ATRP, and the generated hydrophilic polymer PPEGA cannot penetrate through the nanoreactor and is filled in the polymer vesicle. After 24 H of reaction, the conversion rate of polymer PPEGA can reach 40%, and the molecular weight is Mn=3000 g/mol,-D=1.55. When free HRP was used as catalyst, the conversion of PPEGA was 12% lower, the molecular weight Mn could reach 3400 G/mol, and the -D was 1. 18.
When enzyme is used as nanoreactor, its internal confined space can effectively promote the contact between catalyst and substrate, thus it can improve the reaction rate and inhibit the occurrence of side reactions. In addition, its unique cavity structure can provide a personalized reaction site for polymerization, realize the regulation of the structure and configuration of the reaction products, and help to understand the catalysis and reaction process at the molecular level. The whole protein nanoreactor, which combines the advantages of nanoreactor and enzyme-catalyzed polymerization, provides a new idea for improving the size and chemical selectivity of polymerization (such as improving the substrate selectivity according to the pore size of protein capsid) and realizing the folding of specific polymer structures.It lays a practical foundation for the application of enzyme-catalyzed living radical polymerization in the fields of biomedicine, food-grade materials and microelectronic devices.
Protein capsid has a specific pore size, which allows molecules of different sizes to selectively penetrate, while its cavity structure can load and release macromolecules, and make macromolecules fold in the cavity to form a specific nanostructure. Based on the characteristics of protein capsid, Bruns et al. Constructed a protein capsid thermal polymerization (THS) nanoreactor with hollow nanostructure, and cross-linked the HRP catalyst modified by nicotinamide on the inner wall of THS to obtain a nanoreactor with all-protein structure[69]. ATRP was carried out with PEGA as monomer, HEBIB as initiator, NaAsc as reducing agent, water and tetrahydrofuran (7 ∶ 3 V/V) as mixed solvent. By adjusting the fixed/free state of the enzyme, the polymer with controllable molecular weight and dispersity (fixed :conversion=6%,Mn=4400 g/mol,-D=1.08; Free :conversion=18%,Mn=43,700 g/mol,-D=1.23). The large difference in conversion rate and molecular weight may be due to the selective permeability of the protein capsid.
Hydrogel is a kind of hydrophilic three-dimensional network polymer formed by chemical and physical crosslinking, which has good biocompatibility and permeability, and has a good development prospect in the field of biomedicine. Biomimetic and natural enzymes encapsulated in hydrogel systems have high stability and efficient catalytic ability, which can ensure higher loading and better substrate mobility, and have become a hot research topic in the field of biology. Nanoscale hydrogels have great potential for in vivo biological applications due to their dimensional stability and load transport.
Qigang Wang et al. Constructed a metal-coordinated polymer nanogel (SiO2@MPGs) based on the ATRP polymerization system of biocompatible N-acrylic acid-L-lysine monomer catalyzed by HRP and the cross-linking reinforcement of Fe (II) (Fig. 3A)[70]. The nanogel grid has a two-amino acid system with iron as a metal complex, which provides a basis for its realization to mimic enzyme activity. Compared with HRP, it has a similar two-electron catalytic mechanism and a Fe (Ⅲ) complex intermediate with high oxidation ability, and does not produce · OH during the catalytic process. SiO2@MPGs can achieve high catalytic efficiency both in vivo and in vitro, and the fluorescence imaging mechanism of its catalytic high reactive oxygen species (ROS) response is shown in Scheme 3B, which is closely related to its unique structure. After intravenous injection of simulated enzyme and other reagents, no tissue injury and inflammation were observed in various tissues and organs of mice, indicating the biological safety of nanogels.

3 Hemoglobin

Hemoglobin (Hb) is the main component of vertebrate red blood cells, which is composed of four peptide chains connected by non-covalent bonds, each chain has a ferrous heme. The heme is located in a spherical structure (globin) formed by the mutual coiling and folding of peptide chains, and the ferrous ion in the active center is connected with the nitrogen atoms on the four pyrrole rings in the porphyrin ring and the nitrogen atoms in the histidine residue through covalent bonds. Like HRP, the Fe element in the metal center of Hb has obvious oxidation-reduction property and can change among the valence States of Ⅱ, Ⅲ and Ⅳ[71⇓~73]. Hb has a cysteine residue, and the thiol group of cysteine acts as a chain transfer agent, forming a sulfur-centered free radical that initiates the growth of new chains to form protein-polymer conjugates. In the process of free radical polymerization, Hb is often maleated to produce thioether bonds that are not easily attacked by free radicals, blocking cysteine and inhibiting chain transfer, which makes the process of free radical polymerization catalyzed by Hb more complex. Hb catalyzes free radical polymerization, which has significant biocompatibility and medical properties, and can be used to detect the content of hemoglobin in serum or urine. This method can replace the toxic potassium cyanide reagent, so that the polymerization process has the characteristics of green, sustainable and environmentally friendly[74].
Maleamidated Hb has atom transfer radical polymerase (ATRPase) activity, is able to catalyze the ATRP of vinyl monomers, and shows selectivity for the monomer. Bruns et al. Catalyzed the ATRP of NIPAAm, PEGA and poly (ethylene glycol) methacrylate (PEGMA), respectively, using HEBIB and BPN as initiators and AscA as a reducing agent (Scheme 4)[75]. The polymerization of NIPPAm followed first-order kinetics with 73% monomer conversion within 4 H. When the reductant was completely consumed, the polymerization stopped and started again with the addition of AscA. However, the polymerization showed an uncontrollable phenomenon, that is, the molecular weight decreased (Mn up to 292 500 G/mol) and the dispersion increased (-D = 1. 73 ~ 2. 50), which may be caused by irreversible chain termination. However, the polymerization process of PEGA and PEGMA was controllable. When the molecular weight of PPEGA and PPEGMA was 6200 ~ 6500 G/mol, the -D of PPEGA increased from 1.14 to 1.42, while the -D of PPEGMA was not more than 1.17. The initial initiation of PEGA polymerization is slow, and it may be necessary to undergo some structural changes caused by interactions between the protein, monomer, and polymer before Hb can effectively mediate PEGA polymerization.
Enzymes are specific and environmentally sensitive, and their catalytic activity can be regulated by changing the environmental factors such as temperature, pH value and monomer type of ATRP system. Bruns et al. Developed a precisely regulated Hb-catalyzed surface-initiated ATRP (SI-ATRP) method by taking advantage of the selectivity of the enzyme for the environment (Scheme 5)[76]. The surface of silicon wafer was modified by 2-bromoisobutyryl bromide (BiB), and the thermosensitive PNIPAm and PPEGA polymer brushes were synthesized in NaAsc and acetate buffer solution. It was found that Hb showed different avidity for different monomers/polymers. The PPEGA polymer brush has a repulsive effect on Hb, so the formation and growth of PPEGA on the surface is slow during the SI-ATRP process, and then the PNIPAm layer can continue to grow on the PPEG surface through multi-step polymerization. The PNIPAm polymer brush with low critical temperature (LCST) can regulate the protein affinity of the polymer brush surface through temperature, and realize the adsorption and repulsion of Hb through the collapse and extension of the molecular chain at different temperatures, thus regulating the polymerization. At the same time, the total polymerization rate of multi-step SI-ATRP can be adjusted by adjusting the pH value of the system to affect the folding structure of the protein.
Enzymes as catalysts can not only be used in SI-ATRP in aqueous media, but also can precisely regulate the process of SI-ATRP by adjusting the physical and chemical properties of its surface, especially the affinity of Hb protein on its surface. It lays a solid foundation for exploring the interfacial interaction between the surface and biomolecules with catalytic activity and realizing the controllable functionalization of materials.
As a metalloprotein structure, the enzyme has a typical metal active center in its structure, which can replace the transition metal to participate in the eATRP process. eATRP is an improved ATRP developed in recent years, which electrochemically reduces high-valence transition metals to low-valence States, reduces the amount of metal catalyst to ppm, and makes the catalytic process more efficient[77]. Sun Yue et al. studied enzyme-assisted eATRP and successfully synthesized protein imprinted polymer (PIP) (Fig. 2)[78]. Poly (toluidine blue) (PTB) modified glassy carbon electrode (GCE) was coated with a layer of nano-platinum (nPt) to form GCE/PTB/nPt cathode, and saturated calomel electrode and platinum wire were used as reference electrode and counter electrode, respectively, in phosphate buffered saline (PBS, pH = 7). Through electrochemical control, Fe (Ⅲ) in hemoglobin can be reduced to Fe (Ⅱ) at the reaction potential of-0. 51 V to form reduced hemoglobin, which can catalyze the ATRP of Hb to PIP. Because the reaction does not need toxic transition metal as a catalyst or a reducing agent, the influence of the catalyst and the reducing agent on the polymerization reaction is avoided, and the method has wide application prospect in the preparation of biological functional materials, biosensors and the like.
Myoglobin (Mb), composed of a peptide chain and a heme prosthetic group, is mainly distributed in cardiac and skeletal muscle tissues and has the same active center as Hb. Mb-catalyzed SI-ATRP was developed by Hajizadeh et al. Thermosensitive polymer brushes were synthesized by random copolymerization (Si @ P (NIPA-co-APMA)) and block copolymerization (Si @ PNIPA-b-PAPMA) of NIPA and N- (3-aminopropyl) methacrylamide (APMA) on the surface of initiator functionalized silicon[79]. In the polymerization process, a part of Mb is used as a catalyst to catalyze the polymerization reaction; The other part directly reacts with the initiator (-Br) in the form of covalent or non-covalent bonds to prevent the reaction. This is also one of the reasons for the inhomogeneity of the graft copolymer. At the same time, due to the thermal sensitivity of PNIPA, when the temperature rises to 40 ℃, its chemical structure will change, the brush will "collapse" and the size will decrease by 16%. However, the size of copolymer Si @ P (NIPA-co-APMA) increases by 7% when the temperature increases, because the PNIPA chain becomes hydrophobic and the cationic groups in the brush produce strong Coulomb repulsion, which inhibits the thermally induced chain collapse. The synthesis of Mb-catalyzed core-shell nanocopolymers broadens their applications in biomedical fields such as drug delivery.

4 Heme and its derivative mimetic enzymes

Heme is the prosthetic group of HRP, Hb and other enzymes, which is composed of a tetrapyrrole ring and a ferrous ion, also known as heme, and its structure is shown in Figure 6. Ferrous heme is oxidized, and the iron ion becomes III valent, at which time the porphyrin iron complex becomes ferriheme with a positive charge of one unit. In order to make it electrically neutral, the iron ion (III) in heme is usually combined with a chloride ion, hemin. When the chloride ion is replaced by a hydroxyl group, it is hydroxyheme. Metalloproteinases (such as HRP, Hb, etc.) Are usually only suitable for catalyzing monomer polymerization in aqueous phase and are easily inactivated in organic phase, but heme just avoids this, and it can replace HRP to catalyze ATRP of NIPAAm[80]. Heme also has good acid resistance and can catalyze the polymerization of acidic monomers[81]. Ferriheme is the most common type of heme, which has the same green and non-toxic characteristics as enzyme, and can be used as a mimic enzyme to catalyze ATRP.
Kadokawa et al. Used heme instead of HRP as a catalyst, ethyl 2-bromobutyrate (EBB) as an initiator, and Asc as a reducing agent to catalyze NIPAAm for ATRP in a mixed solvent of DMF/H2O. The predicted mechanism is shown in Figure 7. Heme (Fe (III)) is reduced by Asc to heme (Fe (II)), which then reacts with the initiator to form an initial free radical, and the resulting dormant form (Fe (III)) is reduced again by Asc in this cycle to[80]. The reaction was carried out at room temperature, and after 24 H, the conversion rate reached 80%, and the theoretical molecular weight was measured to be Mn=31 800 g/mol,-D=1.80. During the whole polymerization process, -D was maintained at 1.70 ~ 2.00. The results showed that heme could replace HRP to catalyze the ATRP of NIPAAm monomer, but the polymerization process was still poorly controllable. Improving the controllability of heme-catalyzed vinyl monomer ATRP is a major challenge in the future.
A large number of studies have shown that acidic monomers, such as methacrylic acid (MAA), are not suitable for ATRP process, because in acidic environment, there will be reactions that are not conducive to polymerization, such as carboxylic acid may replace the halogen in the catalyst. Enzymes also have the best activity to catalyze monomer polymerization only under the appropriate pH conditions. Heme has good acid resistance and is the best catalyst for acidic monomers. In 2018, Matyjaszewski et al. Studied the ATRP of MAA catalyzed by hemin in H2O/DMF mixed solution (Figure 8 a)[81]. In order to improve the water solubility of heme, it was modified with two polyethylene glycol monomethyl ether (MPEG550), and sufficient amount of dormant Fe (Ⅲ) -Br was obtained by adding excessive NaBr. The structure of the modified heme is shown in Fig. 8B. With α-bromophenylacetic acid (BPAA) and poly (ethylene glycol) 2000 methyl ether-α-bromophenylacetate (PEG2kBPA) (Scheme 8C) as initiators and 0.2 M NaBr added, the conversion was 31% and 39%, respectively, and the measured molecular weight Mn were 7800 G/mol and 10,300 G/mol, which were close to the theoretical values, and -D were 1.44 and 1.55, respectively, after 4 H of reaction. The results show that the reaction is controllable. On this basis, a PEG-b-PMAA-b-POEOMA500 triblock copolymer was synthesized by using PEG2k-b-PMAA-Br(Mn=22 400 g/mol) as macroinitiator and polyethylene glycol monomethyl ether methacrylate (OEOMA500) as monomer, with molecular weight Mn of 84 600 G/mol and -D of 1. 63. It was proved that hemin could catalyze the polymerization of MAA monomer, and the chain end functional groups of the obtained polymer had high fidelity.
DhHP-6 is a heme-containing peroxidase mimetic composed of six amino acid residues and an iron porphyrin, which is a kind of synthetic material with enzymatic activity (Fig. 9a). DhHP-6 has high oxidoreductase activity and can adapt to a wide range of pH (3.0 ~ 11.0), so it can catalyze many kinds of monomers. In most cases, DhHP-6 is used in heterogeneous solution and can be recycled, so it is a potential artificial catalyst. In 2015, Tang et al. Applied DhHP-6 to ATRP to catalyze ARGET ATRP of PEGMA500 in buffer solution with pH = 3.0 – 11.0 (Fig. 9 B)[82]. The molecular weight of the resulting polymer increased linearly with monomer conversion, and -D was relatively low. ATRP was also combined with enzymatic ring-opening polymerization (eROP) to form three types of biodegradable block copolymers (PCL-b-PGMA, PCL-b-PMAA and PCL-b-PHEMA), among which GMA monomer had the best controllability in polymerization, while MAA and HEMA had the worst controllability in polymerization.
However, there are still some problems when DhHP-6 is used as a catalyst, for example, DhHP-6 is easy to self-polymerize in the catalytic process; The activity of DhHP-6 is easy to decrease after long-term storage. In order to improve these problems, Tang et al. Embedded porphyrin imidazole ester scaffold 8 (ZIF-8) into DhHP-6 to obtain composite DhHP-6 @ ZIF-8 (Fig. 3), and carried out PEGMA500 ATRP at 30 ° C with BPN as the initiator[83]. The reductant reduces DhHP-6 @ ZIF-8 from the stable Fe (Ⅲ) to the low valence Fe (Ⅱ), and then reacts with the alkane initiator to form the initial radical (Pn ·) and the dormant species Fe (Ⅲ) -Br. The cycle is repeated to establish the equilibrium between the radical and the dormant species. The results showed that the catalytic controllability was significantly improved after DhHP-6 immobilization, and the monomer conversion rate reached 76.1%,Mn and reached 45,900 G/mol.

5 Laccase

Laccase from T. versicolor is a redox enzyme with Cu ion as the active center, which is widely used in radical polymerization. Compared with peroxidase, the polymerization system of laccase is very simple, which does not need to add additional oxidants, and directly uses oxygen to participate in redox reaction to catalyze polymerization. The structure is shown in Fig. 10a, which is generally composed of a single polypeptide of 500 amino acids, containing four Cu (II) prosthetic groups (type I Cu2+, type II Cu2+, and two type III Cu2+), and exists in the form of a monomeric glycoprotein. The type II Cu2+ and two type III Cu2+ form a cluster and are linked together with the type I Cu2+ by histidine-cysteine-histidine (His-Cys-His). In the reaction process, the most prominent feature of laccase is that oxygen replaces H2O2 as an oxidant, but oxygen can also inhibit the reaction. Some scholars say that it may be the inhibition of oxygen that hinders the wide application of laccase[84].
In 2011, di Lena et al. Studied the effect of different initiators on the ATPR of PEGMA catalyzed by laccase with vitamin C as reducing agent[45]. The polymerization mechanism is shown in Figure 10B. The alkyl halide initiator reacts with the reducing agent under the catalysis of the enzyme to generate an initial free radical, which is further polymerized with the monomer. When EBiB was used as initiator, the monomer conversion reached 20%, the molecular weight Mn was 272 000 G/mol, and -D was 2. 43 in 1 H. After 2 H, the viscosity of the system increased. When 2BPN and ethyl iodoacetate (EIAc) were used as initiators, the polymerization rate of the former was accelerated, and the conversion rate reached 28% after 30 min, while the conversion rate of the latter reached 15% after 22 H, and its dispersion degree was higher, reaching more than 1. 94. The results showed that the monomer conversion was low and the polymer dispersion was high under the action of the three initiators. The poor controllability of laccase-catalyzed ATRP further explains the lack of application of laccase in the field of ATRP.
Because of the specificity of enzymes, different enzymes have different selectivity for monomers. Since di Lena et al. Took the lead in studying the catalytic effect of different enzymes, in 2014, Ko et al. Also studied and compared the SI-ATRP of NIPAM catalyzed by HRP, laccase and catalase at room temperature, respectively, and realized the application of laccase to the surface grafting modification of solid material lignin for the first time, and obtained PNIPAM polymer brush (Mn=1×106g/mol,-D<1.30) with a thickness of more than 100 nm[46][85]. In the experiment, AscA was used as the reducing agent and pure water as the solvent. The concentration of the reducing agent directly affected the grafting efficiency of PNIPAM polymer brushes. The grafting density of polymer brushes increased with AscA concentration from 1.42×10-5 to 5.68×10-5mol/L,PNIPAM (72 ± 19 nm to 113 ± 16 nm). When the concentration of AscA was increased to 14.18×10-5mol/L, the grafting thickness of PNIPAM polymer brush decreased to 67 ± 21 nm. At the same concentration of AscA (5.68×10-5mol/L), the grafting thickness of PNIPAM polymer brush was only 10 ± 25 nm and 39 ± 27 nm with HRP and catalase as catalysts, and the dispersion was also wide (1.66 – 2.93; 1.31 – 1.53). However, there was no significant difference in grafting density among the three catalysts, which were all 7.3×10-2~12.39×10-2nm-2.
Poly (N-vinylimidazole) (PNVIm) polymers characterized by imidazole ring have been widely studied in the fields of material science (such as lithium ion batteries) and medicine and biology (such as gene carriers), and their application properties depend on the controllability of molecular weight and dispersion[86][87][88]. However, due to the occurrence of chain termination and chain transfer in the ATRP process of N-vinylimidazole (NVIm), the resulting PNVIm usually has a wide dispersion and poor controllability[89]. In addition, the resulting polymer complexes metal ions so tightly that the metal catalyst of traditional ATRP is difficult to remove from the polymer, which greatly affects the commercial application of PNVIm[90]. In 2016, Bruns et al. Studied the laccase-catalyzed controlled radical polymerization of NVIm, and used the three-dimensional structure of tightly bound copper ions in laccase to avoid the problem that metal ion catalysts are difficult to remove[91]. PNVIm (-D = 1.27 ~ 1.56) with molecular weight Mn of 1600 ~ 9970 G/mol was successfully obtained in acetate buffer solution at pH 4, and the polymerization followed first-order kinetics. On the contrary, the conversion was very low when HRP and Hb were used as catalysts, which may be due to their different catalytic mechanisms from laccase.
Hydrogel can absorb a large amount of water and can be used to load and release water-soluble biological macromolecules. Zhang Qiang et al. First used laccase as a catalyst, PEGA480 as a monomer, NaAsc as a reducing agent, and EBiB as an initiator to synthesize protein-loaded hydrogels by one-pot method (Fig. 11)[92]. By screening three different ligands, it was found that the addition of Tris (2-dimethylaminoethyl) amine (Me6TREN) could reduce the reaction temperature, improve the reaction kinetics, and form a complex with the copper atom in laccase to maintain its good enzymatic activity. The molecular weight of the crosslinking agent poly (ethylene glycol) diacrylate involved in the reaction has a significant effect on the properties of the polymer hydrogel. When the molecular weight was 400 G/mol and the reaction time was 60 min, the conversion rate was 80%, the loading rate of laccase in the hydrogel was 84%, the release rate was 11%, and the water absorption rate of the hydrogel was 294%. When the molecular weight is 1 000 G/mol, the reaction time is 45 min, the conversion rate is 78%, the loading rate of laccase in the hydrogel is 83%, the release rate is 3%, and the water absorption of the hydrogel is 400%. When the laccase-loaded hydrogel was reused in ABTS solution for 6 times, the enzyme activity did not decrease significantly. Hydrogels with excellent loading properties have broad application prospects in protein delivery and water treatment.
Laccase has a metal redox active center capable of electron transfer and a complex protein structure. In unnatural environments, especially in harsh environments or non-aqueous solvents, laccase will undergo structural denaturation and even inactivation. In order to broaden the application of laccase in non-natural environment, Averick et al. Modified laccase by grafting polymer, and studied its stability and activity in different pH values, high temperatures and organic solvents (acetonitrile, tetrahydrofuran and ethanol)[93]. In order to adapt to different environments, hydrophilic monomer polyoxyethylene acrylate (OEOA) and amphiphilic monomers dimethylaminoethyl methacrylate (DMAEMA) and dimethylaminopropylacrylamide (DMAPA) were selected to graft laccase-iBBr (Figure 12). The results showed that the laccase grafted with the copolymer could maintain its activity in the unnatural environment by coating the active center and amino acid chain with the complex chain structure of the polymer. Among them, laccase-PDMAEMA copolymer has the widest application range, which can maintain the stability and activity of enzyme under acidic or alkaline conditions, high temperature (40 ℃ or 50 ℃), ethanol (containing 10% water) and other conditions.
Chlorophyll is a biocatalyst containing Mg2+ ions, and the researchers used copper-based catalysts represented by laccase as a reference to modify chlorophyll with copper to synthesize chlorophyll copper (Figure 13). Bruns et al. Used copper chlorophyllin as catalyst and comonomer, PEG-Br as initiator and NaAsc as reducing agent to catalyze the ATRP of PEGA[94]. Copper chlorophyllin is reduced by NaAsc to form active free radicals, which activate the initiator (as shown in Figure 13), and finally form poly (PEGA-co-chlorophyll) copolymer with controllable chlorophyll content. The reaction was carried out in aqueous phase and followed first-order kinetics, and the molecular weight of the polymer (Mn=4000~5000 g/mol,-D≤1.11) increased with the rise of conversion. The catalytic system has great potential in the preparation of biomedical and solar energy harvesting materials due to its cheap, green and sustainable characteristics.

6 GOx-HRP enzyme-linked catalysis for ATRP initiation

As an efficient radical trap/inhibitor, oxygen can easily react with chain propagation radicals to form stable peroxyl radicals and hydroperoxides to quench the chain propagation reaction[95]. Oxygen tolerance of RDRP, including ATRP, is a significant challenge for this technology. Therefore, it is of great significance to develop new types of ATRP that can be carried out in oxygen-rich systems[96,97]. Matyjaszewski et al. Developed the GOx deoxygenation technology and applied it to simulate the respiratory metabolic process and carry out ATRP. The polymerization process has good oxygen tolerance and controllability[98]. GOx deoxygenation technology has good universality and can be used in other RDRP including ATRP. For example, An et al applied GOx and pyranose oxidase (P2Ox) catalytic deoxygenation to the RAFT polymerization of water-soluble monomers catalyzed by HRP/H2O2/ACAC ternary system[99⇓~101]. Tan et al. Applied GOx catalytic deoxygenation to photoinduced RAFT polymerization-induced self-assembly[102⇓⇓~105].
The GOx-HRP enzyme-linked catalytic system does not directly participate in the catalysis of ATRP, but can be used as an initiation system to generate free radicals, realize the reduction of metal catalysts, and be applied to improve ATRP. In 2018, Matyjaszewski et al. Developed a biocatalytic system composed of GOx-HRP and active copper (ppm grade) to carry out a novel enzymatic ICAR-ATRP in an open environment, which realized the controlled polymerization of oligo (ethylene oxide) methyl ether methyl methacrylate (OEOMA500)[106]. The polymerization mechanism is shown in Fig. 14. Glucose is oxidized by GOx under the action of oxygen to generate glucolactone and H2O2, and H2O2 reacts with ACAC under the action of HRP to generate ACAC radical, which participates in the redox of copper and carries out the chain propagation process. The reaction proceeded within 1 H to synthesize a polymer with high molecular weight and low dispersity (Mn>70 000 g/mol,1.13≤-D≤1.27). Studies have shown that sufficient oxygen contributes to the generation of free radicals and the extension of polymer chains. GOx-HRP was used as an initiation system to realize the synthesis of bioconjugates (protein-b-POEOMA, DNA-b-POEOMA) with protein and DNA as templates, which provided a basis for the synthesis of materials with good biocompatibility. Lv et al. Also applied GOx-HRP to the preparation of biosensors, and prepared pH-responsive imprinted polymers by SI-ATRP[107]. It can be used to detect the concentration of glucose in serum clinically, which is of great significance to assist the diagnosis of diabetes and hypoglycemia and to detect the response to treatment.

7 Conclusion and prospect

In this paper, the latest progress in the study of enzyme-catalyzed ATRP in recent years was systematically summarized, and the enzymes were classified according to the active metal center, and the enzyme-catalyzed initiation system, monomer, reaction conditions, and polymerization mechanism were introduced in detail. Enzymatic catalysis, as a new type of catalytic system, has the advantages of green, efficient, environmentally friendly, wide range of suitable monomers, preparation of polymers with special molecular configurations, and convenient oxygen removal.The application of enzyme catalytic system provides an efficient and convenient way to expand the range of suitable monomers for ATRP and stably prepare polymers/copolymers with special and complex structures. At the same time, enzyme-catalyzed ATRP can be used as a green and non-toxic biological detection method because of its good biocompatibility and even living cell modification compatibility, which has great potential in the biomedical field. In addition, enzyme-catalyzed ATRP also has the advantages of mild polymerization conditions, high efficiency of polymerization process and stereoselectivity, controllable reaction process and final product structure, and green sustainability.
Enzyme-catalyzed controlled radical polymerization is in the stage of rapid development. In recent years, the development of new photoenzymatic controlled radical polymerization technology has provided new inspiration for the preparation of molecular weight controlled and ultra-high molecular weight polymers by enzyme-catalyzed controlled radical polymerization[108,109]. In the future, it is of great significance for enzyme-catalyzed ATRP to develop more enzyme-catalyzed systems with high activity to broaden the range of monomer selection, improve the controllability of polymerization and synthesize ultra-high molecular weight polymers. In addition, it is also of great research value to develop a continuous flow enzyme-catalyzed polymerization system by combining enzyme catalysis with microflow field technology through immobilized enzyme technology, and to prepare new functional polymers with complex structures in high throughput.

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Funding

National Key R&D Program of China(2019YFA0905000)

National Natural Science Foundation of China(21604037)

Jiangsu Synergetic Innovation Center for Advanced Bio-Manufacture(XTD1823)

Jiangsu Synergetic Innovation Center for Advanced Bio-Manufacture(XTB1802)

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