Metal ion interactions with drugs: Electrochemical study of complexation of various bivalent metal ions with nimesulide and ibuprofen

2013 ◽  
Vol 182 ◽  
pp. 39-42 ◽  
Author(s):  
H. Kaur ◽  
J.K. Puri ◽  
Anita Singla
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Electrochemical Study ◽  
Bivalent Metal ◽  
Ion Interactions ◽  
Bivalent Metal Ions ◽  
Metal Ion Interactions

Degradation of Perfluoropolyether Fluids With Metal Ions

1999 ◽  
Vol 121 (2) ◽  
pp. 348-351 ◽  
Author(s):  
Takashi Fukuchi
Keyword(s):  
Metal Ions ◽  
Reaction Mechanisms ◽  
Metal Ion ◽  
Chemical Degradation ◽  
Bivalent Metal ◽  
Ether Cleavage ◽  
Cleavage Process ◽  
Metal Atoms ◽  
Bivalent Metal Ions ◽  
Fomblin Z

Chemical degradation of lubricant fluids of perfluoropolyether (PFPE), such as Fomblin Z-DOL, Fomblin AM-2001, Fomblin Z-25, Demnum SP-3, and Demnum SA, with bivalent metal ions was examined. The respective reaction mechanisms involve an ether cleavage process which is caused by the coordination of metal ions with oxygen atoms in the main chains of the PFPE. Metal ions were evaluated for their ability to degrade the PFPE, and the results demonstrate that the ions ranking in terms of this ability is as follows: Cu2+ > Ni2+ > Co2+ > Fe2+ > Mn2+ > Mg2+. This trend can be explained by the ionization potentials of the metal atoms. For an identical metal ion, the Demnum lubricants showed a greater stability than the Fomblin lubricants.

DNA-bound metal ions: recent developments

2014 ◽  
Vol 5 (5) ◽  
pp. 397-407 ◽  
Author(s):  
Daniel L. Morris
Keyword(s):  
Dna Damage ◽  
Metal Ions ◽  
Recent Work ◽  
Conformational Changes ◽  
Metal Ion ◽  
Oxidative Dna Damage ◽  
Logic Gates ◽  
Base Pairing ◽  
Ion Interactions ◽  
Metal Ion Interactions

AbstractThe affinity of metal ions for DNA is logical considering that the structure of DNA includes a phosphate backbone with a net-negative charge, a deoxyribose sugar with O atoms, and purine and pyrimidine bases that contain O and N atoms. DNA-metal ion interactions encompass a large area of research that ranges from the most fundamental characterization of DNA-metal ion binding to the role of DNA-bound metal ions in disease and human health. Alternative DNA base pairing mediated by metal binding is also being investigated and manipulated for applications in logic gates, molecular machines, and nanotechnology. This review highlights recent work aimed at understanding interactions of redox-active metal ions with DNA that provides a better understanding of the mechanisms by which various types of oxidative DNA damage (strand breakage and base modifications) occur. Antioxidants that mitigate oxidative DNA damage by coordinating metal ions that produce reactive oxygen species are addressed, as well as recent work on the effect of DNA-metal ion interactions and the efficacy of quinolone-based antibacterial drugs. Recent advances in metal-mediated base pairing that triggers conformational changes in DNA structure for use as selective metal ion sensors and novel nanotechnology applications are also included.

scholarly journals Activation of membrane-bound high-affinity calcium ion-sensitive adenosine triphosphatase of human erythrocytes by bivalent metal ions

1975 ◽  
Vol 147 (2) ◽  
pp. 359-361 ◽  
Author(s):  
H Pfleger ◽  
H U Wolf
Keyword(s):  
Metal Ions ◽  
Calcium Ion ◽  
Metal Ion ◽  
Adenosine Triphosphatase ◽  
Erythrocyte Membranes ◽  
Bivalent Metal ◽  
High Affinity ◽  
Human Erythrocyte Membranes ◽  
Bivalent Metal Ions ◽  
Membrane Bound

The Ca2+-sensitive ATPase (adenosine triphosphatase) of human erythrocyte membranes is activated, not only by Ca2+ ions, but also by a series of other bivalent metal ions including Sr2+, Ba2+, Mn2+, Ni2+, Co2+, Cd2+, Cu2+, Zn2+ and Pb2+. The degree of activation is dependent on the radius of the ion rather than on its nature, in contrast with the dissociation constant of the enzyme--metal ion complex.

scholarly journals The specificity of yeast low-Km cyclic AMP phosphodiesterase towards free bivalent metal ions and the diastereoisomers of cyclic adenosine phosphorothioate

1985 ◽  
Vol 226 (3) ◽  
pp. 897-900 ◽  
Author(s):  
K Suoranta ◽  
J Londesborough
Keyword(s):  
Cyclic Amp ◽  
Metal Ions ◽  
Metal Ion ◽  
Relative Activity ◽  
Bivalent Metal ◽  
Cyclic Amp Phosphodiesterase ◽  
Bivalent Metal Ions

The relative activity of a zinc-containing cyclic AMP phosphodiesterase towards the (Sp)- compared with the (Rp)-diastereoisomer of cyclic adensine phosphorothioate varied with the identity of the free bivalent metal ion from more than 35 to 0.074 along the series Mg2+ greater than Mn2+ greater than Co2+ greater than Zn2+ greater than Cd2+, showing that this ion, and not the tightly bound zinc, bonds to the phosphorothioate moiety of the substrate.

scholarly journals Metal ion interactions in the control of haem oxygenase induction in liver and kidney

1980 ◽  
Vol 192 (2) ◽  
pp. 637-648 ◽  
Author(s):  
G S Drummond ◽  
A Kappas
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Simultaneous Administration ◽  
Ion Interactions ◽  
Liver And Kidney ◽  
Demethylase Activity ◽  
Haem Oxygenase ◽  
Metal Ion Interactions ◽  
Cytochrome P 450

Mn2+ and Zn2+ exhibit a striking ability to block the induction by Sn2+ and Ni2+ of haem oxygenase (EC 1.14.99.3) in kidney. The blocking effects of Mn2+ and Zn2+ were found to be greatest on simultaneous administration, time-dependent when administered up to 8 h before the inducing metal ions, and ineffective when administered as little as 10 min after the inducing metal ions. The decreases in cytochrome P-450 and haem contents and the sequential changes in delta-aminolaevulinate synthase (EC 2.3.1.37) activity that occur concomitant with haem oxygenase induction were largely eliminated with simultaneous or prior treatment with Mn2+ or Zn2+, but not when Mn2+ or Zn2+ was administered after Sn2+ or Ni2+. Mn2+ and Zn2+ did not increase the catabolism of the enzyme in vivo. Zn2+ on simultaneous administration was also able substantially to block the induction of haem oxygenase by Co2+, Cd2+ and Ni2+ in liver. The Zn2+ blockade of Cd2+ induction was examined in detail, and prior or simultaneous administration of Zn2+ was found to be effective in blocking the induction of haem oxygenase and the concomitant decreases in cytochrome P-450 and haem contents, ethylmorphine demethylase activity and the sequential changes in delta-aminolaevulinate synthase activity. Zn2+ administration 10 min or more after Cd2+ was ineffective in preventing the occurrence of these perturbations in haem metabolism. These findings describe a new and striking biological property of Mn2+ and Zn2+, and indicate the existence of significant metal ion interactions in the control of haem metabolism.

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