Surfactant-histidine-heme ternary complex as a simple artificial heme enzyme in organic media

Kamiya, Noriho; Goto, Masahiro; Furusaki, Shintaro

doi:10.1002/(sici)1097-0290(19990820)64:4<502::aid-bit13>3.0.co;2-h

Cited by 12 publications

(3 citation statements)

References 24 publications

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“…However, this method is applicable to hydrophilic proteins such as chymotrypsin (Abe et al, 1997a) and peroxidase . The extent of enzymatic catalysis in organic media using surfactant-protein complexes with various types of model protein, such as lipase (Huang et al, 1998), peroxidase (Kamiya et al, 1999(Kamiya et al, , 2000Kamiya and Nagamune, 2002;Okazaki et al, 2000aOkazaki et al, , 2001Michizoe et al, 2003Michizoe et al, , 2004, laccase (Okazaki et al, 2000b;Michizoe et al, 2005) and protease (Okazaki et al, 2000c) was investigated. The overall results are shown in Fig.…”

Section: Introductionmentioning

confidence: 99%

Solid-in-oil dispersion: A novel core technology for drug delivery systems

Tahara

Kamiya

Goto

2012

International Journal of Pharmaceutics

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Section: Introductionmentioning

confidence: 99%

Solid-in-oil dispersion: A novel core technology for drug delivery systems

Tahara

Kamiya

Goto

2012

International Journal of Pharmaceutics

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“…[16][17][18] Iron porphyrins are biocatalysts, which catalyze oxidative reactions by decomposing hydrogen peroxide at the expense of various substrates, such as phenols and amides. 19 Thus, a peroxidase-like MIP that efficiently catalyzes the oxidation of 4-aminophenol (4-APh) with considerable substrate specificity in the presence of hydrogen peroxide using a flow injection analysis system coupled to amperometric detection was described. Complementing these results, in the present work, presents the characterization by several physical techniques of the MIP, as well as, parameters such as the specificity, enzyme-mimic activity catalytic effects and Michaelis-Menten kinetics were evaluated.…”

Section: Introductionmentioning

confidence: 99%

Synthesis, characterization and kinetics of catalytically active molecularly imprinted polymers for the selective recognition of 4-aminophenol

Santos¹,

Lima²,

Tarley³

et al. 2009

J. Braz. Chem. Soc.

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No presente trabalho um polímero com impressão molecular (MIP) seletivo para 4-aminofenol (4-APh) foi sintetizado através de técnica de polimerização em bulk. A polimerização foi realizada em tubo de vidro contendo 4-APh, Fe(III)protoporfrina(IX) (hemina, Fe(III)PPIX), ácido metacrílico (MAA), etileno glicol dimetacrilato (EGDMA) e 2,2'-azo-bis-iso-butironitrila (AIBN). O bloco de polímero foi moído e peneirado (106 µm) e o 4-APh foi removido das partículas do polímero pela extração com solução de metanol/ácido acético (4:1, v/v), deixando uma cavidade nas partículas do polímero. A hemina foi usada como um material sintético para imitar o centro ativo da peroxidase, criando um polímero com impressão molecular cataliticamente ativo. Os polímeros foram caracterizados por espectroscopia no infravermelho, análises termogravimétricas, microscopia eletrônica de varredura e análise do tamanho das partículas. O desempenho enzimático do polímero impresso foi avaliado baseado em parâmetros cinéticos incluindo V max e constante de Michaelis-Menten obtidas pelo gráfico de Lineweaver-Burk.In the present work a selective molecularly imprinted polymer (MIP) for 4-aminophenol (4-APh) was synthesized by the bulk polymerization technique. Polymerization was carried out in a glass tube containing 4-APh, Fe(III)protoporphyrin(IX) (hemin, Fe(III)PPIX), methacrylic acid (MAA), ethylene glycol dimethacrylate (EGDMA) and 2,2′-azo-bis-iso-butyronitrile (AIBN). The polymer block was ground and sieved (106 µm) and the 4-APh was removed from the polymer particles by leaching with a methanol/acetic acid (4:1, v/v) solution, which leaves a cavity in the polymer particles. Hemin was used as a synthetic material to mimic the active center of peroxidase creating a catalytically active molecularly imprinted polymer. The polymers were characterized by infrared spectroscopy, thermogravimetric analysis, scanning electron microscopy and particle size analysis. The enzymatic performance of the imprinted polymer was evaluated based on kinetic parameters including V max and the Michaelis-Menten constant obtained from Lineweaver-Burk plots. Keywords: molecularly imprinted polymers (MIP), hemin, 4-aminophenol, MichaelisMenten IntroductionMolecular imprinting is a useful technique for the preparation of ligand-selective cavities in synthetic polymer matrices. [1][2][3] Recently, the technique has attracted significant interest from a large number of areas within chemistry and the analytical sciences due to the relative ease with which these polymers may be prepared, the range of template structures that are amenable for use and the apparent mechanical and chemical stability of the types of polymers generally synthesized.Briefly, the technique may be described as follows. A template molecule is allowed to form reversible interactions (covalent or non-covalent) with suitable functionalized monomers in the presence of a cross-linking monomer. Polymerization affords a highly cross-linked macroporous polymer containing cavities with sites varying complementari...

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“…Arti®cial peroxidase mimics have been also investigated in recent years, and some of these investigations have involved the design and synthesis of porphyrin derivatives. For example, Takahashi et al (1986) prepared a polyethylene glycol-modi®ed hemin that was soluble and exhibited peroxidase activity in several organic solvents; Johnstone et al (1997) synthesized Mn(III)-tetraphenylporphyrin carried in amphiphilic water-soluble polymers and demonstrated that it had peroxidase activity in an aqueous environment; Kamiya et al (1999) demonstrated that a surfactanthistidine-hemin complex showed peroxidase activity in organic media. On the other hand, the generation of hemin-binding antibody was proposed as another approach to obtain arti®cial peroxidase molecules.…”

Section: Introductionmentioning

confidence: 99%

Peroxidase activity of in vitro‐selected 2′‐amino RNAs

Teramoto

Ichinari

Naoki

et al. 2001

Biotech & Bioengineering

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Peroxidase activities of RNAs containing 2'-amino groups, which were selected as aptamers binding to N-methylmesoporphyrin IX, were investigated. Some clones promoted the oxidation reaction of 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) with hydrogen peroxide (H(2)O(2)) in the presence of iron(III)-protoporphyrin (hemin), whereas others did not. Each of them had a different substrate specificity. One of the active clones promoted the oxidation of o-dianisidine and beta-nicotinamide adenine dinucleotide reduced form (NADH) with H(2)O(2) 5 and 15 times faster than hemin only, respectively. On the other hand, one clone that was inactive on oxidation of ABTS exhibited the same level of activity on oxidation of o-dianisidine as that shown by the clone active on ABTS but no activity on NADH. By in vitro selection, we can produce various types of peroxidase-like non-natural RNAs.

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Surfactant-histidine-heme ternary complex as a simple artificial heme enzyme in organic media

Cited by 12 publications

References 24 publications

Solid-in-oil dispersion: A novel core technology for drug delivery systems

Solid-in-oil dispersion: A novel core technology for drug delivery systems

Synthesis, characterization and kinetics of catalytically active molecularly imprinted polymers for the selective recognition of 4-aminophenol

Peroxidase activity of in vitro‐selected 2′‐amino RNAs

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