Improved Anti‐Inflammatory and Pharmacokinetic Properties for Superoxide Dismutase by Chemical Glycosidation with Carboxymethylchitin

Valdivia, Aimara; Pérez, Y.; Domínguez, A.; Caballero, Julio; Gómez, Leissy; Schacht, Etienne; Villalonga, Reynaldo

doi:10.1002/mabi.200400114

Cited by 22 publications

(25 citation statements)

References 31 publications

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“…Later, superoxide dismutase resistance to inactivation by hydrogen peroxide has been greatly improved by glycosidation with carboxymethylchitin. It was explained again by the chelating ability of the polymer, which could bind the Cu 2+ released from the protein structure after oxidation [264].…”

Section: Chemical Modificationmentioning

confidence: 99%

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hernández

Berenguer-Murcia²,

Rodrigues³

et al. 2012

COC

137

107

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Hydrogen peroxide is a substrate or side-product in many enzyme-catalyzed reactions. For example, it is a side-product of oxidases, resulting from the re-oxidation of FAD with molecular oxygen, and it is a substrate for peroxidases and other enzymes. However, hydrogen peroxide is able to chemically modify the peptide core of the enzymes it interacts with, and also to produce the oxidation of some cofactors and prostetic groups (e.g., the hemo group). Thus, the development of strategies that may permit to increase the stability of enzymes in the presence of this deleterious reagent is an interesting target. This enhancement in enzyme stability has been attempted following almost all available strategies: site-directed mutagenesis (eliminating the most reactive moieties), medium engineering (using stabilizers), immobilization and chemical modification (trying to generate hydrophobic environments surrounding the enzyme, to confer higher rigidity to the protein or to generate oxidation-resistant groups), or the use of systems capable of decomposing hydrogen peroxide under very mild conditions. If hydrogen peroxide is just a side-product, its immediate removal has been reported to be the best solution. In some cases, when hydrogen peroxide is the substrate and its decomposition is not a sensible solution, researchers coupled one enzyme generating hydrogen peroxide "in situ" to the target enzyme resulting in a continuous supply of this reagent at low concentrations thus preventing enzyme inactivation.This review will focus on the general role of hydrogen peroxide in biocatalysis, the main mechanisms of enzyme inactivation produced by this reactive and the different strategies used to prevent enzyme inactivation caused by this "dangerous liaison". Outlook

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Section: Chemical Modificationmentioning

confidence: 99%

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hernández

Berenguer-Murcia²,

Rodrigues³

et al. 2012

COC

137

107

View full text Add to dashboard Cite

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“…In the later cases, this reduction could be given by partial inactivation of the enzyme after treatment with the carbodiimide, as has been previously described [24]. It is also evident that reductive alkylation of CAT with MAN strongly affected the catalytic behavior of this enzyme.…”

Section: Resultsmentioning

confidence: 76%

Pharmacokinetics and Stability Properties of Catalase Modified with Water‐Soluble Polysaccharides

Valdivia

Pérez

Gómez

et al. 2006

Archiv der Pharmazie

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Bovine liver catalase (EC 1.11.1.6) was chemically modified with mannan, carboxymethylcellulose, and carboxymethylchitin. The enzyme retained about 48-97% of the initial specific activity after glycosidation with the polysaccharides. The prepared neoglycoenzyme was 1.9-5.7 fold more stable against the thermal inactivation processes at 55 degrees C, in comparison with the native counterpart. Also, the modified enzyme was more resistant to proteolytic degradation with trypsin. Pharmacokinetics studies revealed higher plasma half-life time for all the enzyme-polymer preparations, but better results were achieved for the enzyme modified with the anionic macromolecules.

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“…SOD was remarkably resistant to inactivation by H 2 O 2 and its antiinflammatory activity was 4.5-fold increased after supramolecular association with the modified CAT form. polymers [3][4][5] or chemical conjugation with catalase (CAT, EC 1.11.1.6) has been proposed as useful tools for overcoming these problems. [6] However, few attempts have been reported on the combined use of these strategies.…”

Section: Full Papermentioning

confidence: 99%