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1011-73-0Relevant articles and documents
Imaging of enzyme replacement therapy using PET
Phenix, Christopher P.,Rempel, Brian P.,Colobong, Karen,Doudet, Doris J.,Adam, Michael J.,Clarke, Lorne A.,Withers, Stephen G.
, p. 10842 - 10847 (2010)
Direct enzyme replacement therapy (ERT) has been introduced as a means to treat a number of rare, complex genetic conditions associated with lysosomal dysfunction. Gaucher disease was the first for which this therapy was applied and remains the prototypical example. Although ERT using recombinant lysosomal enzymes has been shown to be effective in altering the clinical course of Gaucher disease, Fabry disease, Hurler syndrome, Hunter syndrome, Maroteaux-Lamy syndrome, and Pompe disease, the recalcitrance of certain disease manifestations underscores important unanswered questions related to dosing regimes, tissue half-life of the recombinant enzyme and the ability of intravenously administered enzyme to reach critical sites of known disease pathology.We have developed an innovative method for tagging acid β-glucocerebrosidase (GCase), the recombinant enzyme formulated in Cerezyme used to treat Gaucher disease, using an 18F-labeled substrate analogue that becomes trapped within the active site of the enzyme. Using micro-PET we show that the tissue distribution of injected enzyme can be imaged in a murine model and that the PET data correlate with tissue 18F counts. Further we show that PET imaging readily monitors pharmacokinetic changes effected by receptor blocking. The ability to 18F-label GCase to monitor the enzyme distribution and tissue half-life in vivo by PET provides a powerful research tool with an immediate clinical application to Gaucher disease and a clear path for application to other ERTs.
Homodinuclear [Fe(III)?Fe(III)] and [Zn(II)?Zn(II)] complexes of a binucleating [N4O3] symmetrical ligand with purple acid phosphatase (PAP) and zinc phosphoesterase like activity
Pathak, Chandni,Gangwar, Manoj Kumar,Ghosh, Prasenjit
, p. 88 - 100 (2018/02/27)
The homodinuclear [Fe(III)–Fe(III)] (2) and [Zn(II)–Zn(II)] (3) complexes of binucleating [N4O3] symmetrical ligand (1) of the formulation, H3L (L = 2,6-bis{[(2-hydroxybenzyl)(2-pyridylmethyl)amino]methyl}-4-t-butylphenolate), display purple acid phosphatase (PAP) and zinc phosphoesterase like activity. For the two complexes, the spectrophotometric titration and the ESI-MS studies supported the existence of an equilibrium between a triaquated species, {L[(H2O)FeIII(μ-H2O)FeIII(H2O)]}3+ (2A) and {L[(H2O)ZnII(μ-H2O)ZnII(H2O)]}+ (3A), a diaquated and monohydroxo species, {L[(H2O)FeIII(μ-H2O)FeIII(OH)]}2+ (2B) and {L[(H2O)ZnII(μ-H2O)ZnII(OH)]} (3B), a monoaquated and dihydroxo species, {L[(H2O)FeIII(μ-OH)FeIII(OH)]}+ (2C) and {L[(H2O)ZnII(μ-OH)ZnII(OH)]}? (3C), and a trihydroxo species, {L[(HO)FeIII(μ-OH)FeIII(OH)]} (2D) and {L[(HO)ZnII(μ-OH)ZnII(OH)]}2? (3D), depending upon the pH of the solution. Of these, the active species namely, a monoaquated and dihydroxo species, {L[(H2O)FeIII(μ-OH)FeIII(OH)]}+ (2C) and {L[(H2O)ZnII(μ-OH)ZnII(OH)]}? (3C), hydrolyzed an activated substrate bis(2,4-dinitrophenyl)phosphate at the pH range of 5.5–10.5, displaying Michealis–Menton kinetics. Significantly enough, the catalyst-substrate adduct of the type {L[FeIII(μ-OH)(μ-RPO4)FeIII]} (2F) has been detected by ESI-MS for the dinuclear [Fe(III)–Fe(III)] complex (2).
Kinetics and mechanism of reactions between 1-N-crown ether-2,4-dinitrobenzenes and alkali metal hydroxides
LESka, BogusLawa,Schroeder, Grzegorz,Gierczyk, BLazej
, p. 461 - 470 (2007/10/03)
The following macrocylic compounds: 1-N-12C4-2,4-dinitrobenzene, 1-N-15C5-2,4-dinitrobenzene and 1-N-18C6-2,4-dinitrobenzene were synthesized. Kinetics and spectroscopic studies of reactions between these compounds and alkali metal hydroxides (LiOH, NaOH, KOH, RbOH and CsOH) in mixed solvent DMSO water (95:5 v/v) were investigated. The results were compared to analogous reactions of 1-X-2,4-dinitrobenzenes. These studies show that the kinetics of the formation of both 3-hydroxy complex and phenolate ions depend strongly on the size of the cation. The formation of the stable complex of cations and 1-N-crown ether-2,4-dinitrobenzene increases the rate constant of formation of both 3-hydroxy complex and phenolate ions. The process of complex formation between the alkali metal cation and macrocylic compounds in mixed solvent DMSO : water is very fast and precedes the nucleophilic attack of hydroxide ion on the benzene ring.