Laccase-catalyzed controlled radical polymerization of N-vinylimidazole

Fodor, Csaba; Gajewska, Bernadetta; Rifaie‐Graham, Omar; Apebende, Edward A.; Pollard, Jonas; Bruns, Nico

doi:10.1039/c6py01261b

Cited by 46 publications

(43 citation statements)

References 79 publications

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“…27,28 Moreover, surface-initiated enzymatic polymerizations of DNA by terminal deoxynucleotidyl transferase have been explored to amplify signals in biosensing. [29][30][31][32][33][34] Recently, we and others have shown that metalloproteins such as hemoglobin (Hb), horseradish peroxidase, and laccase can catalyze ATRP in solution [35][36][37][38][39][40][41][42] and on surfaces. 39,43,44 These biocatalysts represent a biocompatible, nontoxic and environmentally friendly alternative to conventional, transition metal-based ATRP catalysts.…”

Section: Introductionmentioning

confidence: 99%

Controlling Enzymatic Polymerization from Surfaces with Switchable Bioaffinity

et al. 2017

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The affinity of surfaces toward proteins is found to be a key parameter to govern the synthesis of polymer brushes by surface-initiated biocatalytic atom transfer radical polymerization (SI-bioATRP). While the "ATRPase" hemoglobin (Hb) stimulates only a relatively slow growth of protein repellent brushes, the synthesis of thermoresponsive grafts can be regulated by switching the polymer's attraction toward proteins across its lower critical solution temperature (LCST). Poly(N-isopropylacrylamide) (PNIPAM) brushes are synthesized in discrete steps of thickness at temperatures above LCST, while the biocatalyst layer is refreshed at T< LCST. Multistep surface-initiated biocatalytic ATRP demonstrates a high degree of control, results in high chain end group fidelity and enables the synthesis of multiblock copolymer brushes under fully aqueous conditions. The activity of Hb can be further modulated by tuning the accessibility of the heme pocket within the protein. Hence, the multistep polymerization is accelerated at acid pH, where the enzyme undergoes a transition from its native to a molten globule conformation. The controlled synthesis of polymer brushes by multistep SI-bioATRP highlights how a biocatalytic synthesis of grafted polymer films can be precisely controlled through the modulation of the polymer's interfacial physicochemical properties, in particular of the affinity of the surface toward proteins. This is not only of importance to gain a predictive understanding of surface-confined enzymatic polymerizations, but also represents a new way to translate bioadhesion into a controlled functionalization of materials.

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Section: Introductionmentioning

confidence: 99%

Controlling Enzymatic Polymerization from Surfaces with Switchable Bioaffinity

et al. 2017

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“…Among those is the conductive polymer polyaniline (PANI), the laccase-mediated synthesis of which was outlined in a recent review [149]. The atom transfer radical polymerization of N-vinylimidazole catalyzed by T. versicolor laccase showcased its ability to produce a polymer with a well-defined molecular mass and potential applications in drug and gene delivery, fuel cell membranes, and polyionic liquids [150]. Another laccase-mediated polymerization in a highly controlled manner produced alternating copolymers of catechol and xylylenediamines with potential applications as imaging agents [151].…”

Section: Plastics and Biopolymersmentioning

confidence: 99%

Applications of Microbial Laccases: Patent Review of the Past Decade (2009–2019)

et al. 2019

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There is a high number of well characterized, commercially available laccases with different redox potentials and low substrate specificity, which in turn makes them attractive for a vast array of biotechnological applications. Laccases operate as batteries, storing electrons from individual substrate oxidation reactions to reduce molecular oxygen, releasing water as the only by-product. Due to society’s increasing environmental awareness and the global intensification of bio-based economies, the biotechnological industry is also expanding. Enzymes such as laccases are seen as a better alternative for use in the wood, paper, textile, and food industries, and they are being applied as biocatalysts, biosensors, and biofuel cells. Almost 140 years from the first description of laccase, industrial implementations of these enzymes still remain scarce in comparison to their potential, which is mostly due to high production costs and the limited control of the enzymatic reaction side product(s). This review summarizes the laccase applications in the last decade, focusing on the published patents during this period.

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“…Yet, enzymatic catalysis works not only in vivo, but also for biological or even synthetic polymers in vitro . In the presence of a suitable substrate, some enzymes like horseradish peroxidase (HRP) or laccase produce radical species as byproducts, which can be utilized as environmentally friendly initiators for radical polymerizations . The mechanism of HRP‐mediated radical polymerization is well known, and also sketched in Figure .…”

Section: Introductionmentioning

confidence: 99%

Enzyme‐Mediated In Situ Buildup and Site‐Specific Addressing of Polymeric Coatings

Appel

Wedegärtner

Lüther

et al. 2018

Macro Materials & Eng

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Formation of site‐specific deposition of polymeric particles and films with controllable parameters via enzyme‐mediated addressing is investigated. The polymers are synthesized in situ by combining the addressing process with enzyme‐mediated radical polymerization, using the enzyme horseradish peroxidase. As a model system, the technically important poly(methyl methacrylate) is formed and addressed on both glass‐ and polyethylene supports.The key to the controllability is the influence of different reaction parameters on particle formation, namely, the concentration of H2O2 and the pH show the most significant impact. With higher concentrations of H2O2, size and amount of gained particles increases, due to H2O2 being a limiting factor to the reaction. Moreover, since acetyl acetone forms the end‐group of the polymer chains, the pH directly influences the particle stability in addition to affecting the enzyme activity. This effect can be utilized to gain either films or particle assemblies at will. Deposition occurs highly site‐specific, exclusively on enzyme‐functionalized areas, enabling patterned coating structures within a safe, energy efficient, and easy‐to‐apply process.

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Laccase-catalyzed controlled radical polymerization of N-vinylimidazole

Abstract: Laccase from Trametes versicolor catalyzes the controlled radical polymerization of N-vinylimidazole, yielding narrowly dispersed, metal-free polymers.

Cited by 46 publications

References 79 publications

Controlling Enzymatic Polymerization from Surfaces with Switchable Bioaffinity

Controlling Enzymatic Polymerization from Surfaces with Switchable Bioaffinity

Applications of Microbial Laccases: Patent Review of the Past Decade (2009–2019)

Enzyme‐Mediated In Situ Buildup and Site‐Specific Addressing of Polymeric Coatings

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