Fluorescent signaling provides deeper insight into aromatic anion uptake by metal-ion activated molecular receptors

MetLigDB (http://silver.sejong.ac.kr/MetLigDB) is a publicly accessible web-based database through which the interactions between a variety of chelating groups and various central metal ions in the active site of metalloproteins can be explored in detail. Additional information can also be retrieved, including protein and inhibitor names, the amino acid residues coordinated to the central metal ion, and the binding affinity of the inhibitor for the target metalloprotein. Although many metalloproteins have been considered promising targets for drug discovery, it is difficult to discover new inhibitors because of the difficulty in designing a suitable chelating moiety to impair the catalytic activity of the central metal ion. Because both common and specific chelating groups can be identified for varying metal ions and the associated coordination environments, MetLigDB is expected to give users insight into designing new inhibitors of metalloproteins for drug discovery.

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Immobilized metal-ion affinity systems for recovery and structure–function studies of proteins at molecular, supramolecular, and cellular levels

Pure and Applied Chemistry ◽

10.1351/pac-con-09-01-18 ◽

2010 ◽

Vol 82 (1) ◽

pp. 39-55 ◽

Cited By ~ 8

Author(s):

Rajasekar R. Prasanna ◽

Mookambeswaran A. Vijayalakshmi

Keyword(s):

Capillary Electrophoresis ◽

Recombinant Proteins ◽

Gel Electrophoresis ◽

Metal Ion ◽

Immobilized Metal Affinity Chromatography ◽

Metal Affinity ◽

Purification Technique ◽

Affinity Gel Electrophoresis ◽

Insight Into ◽

Histidine Tag

Immobilized metal-ion affinity (IMA) adsorption is a collective term that is used to include all kinds of adsorptions where the metal ion serves as the characteristic and most essential part of adsorption center. Of all the IMA techniques, immobilized metal-affinity chromatography (IMAC) has been gaining popularity as the choice of purification technique for proteins. IMAC represents a separation technique that is primarily useful for proteins with natural surface exposed-histidine residues and for recombinant proteins with engineered histidine tag. This review also gives insight into other nonchromatographic applications of IMA adsorption such as immobilized metal-ion affinity gel electrophoresis (IMAGE), immobilized metal-ion affinity capillary electrophoresis (IMACE), and immobilized metal-ion affinity partitioning (IMAP).

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Metal ion – biomolecule interactions. X. Synthesis, spectroscopic and magnetic resonance investigations of methylmercury(II) complexes of the sulfur modified nucleosides 6- mercaptopurine riboside and 2-amino-6-mercaptopurine riboside

Canadian Journal of Chemistry ◽

10.1139/v86-069 ◽

1986 ◽

Vol 64 (3) ◽

pp. 442-448 ◽

Cited By ~ 15

Author(s):

E. Buncel ◽

R. Kumar ◽

A. R. Norris

Keyword(s):

Aqueous Solution ◽

Metal Ion ◽

Chemotherapeutic Agents ◽

Modified Nucleosides ◽

Coupling Constants ◽

Heterocyclic Ligands ◽

Methylmercury Poisoning ◽

Insight Into ◽

C Nmr ◽

Ligand Bond

A number of methylmercurated complexes of 6-mercaptopurine riboside and 2-amino-6-mercaptopurine riboside (6-MNucH2) containing S-bound CH3Hg(II) in neutral and cationic complexes (as in [CH3Hg(6-MNucH)] and [CH3Hg(6-MNucH2)]NO3), S- and N-bound CH3Hg(II) (as in [(CH3Hg)2(6-MNucH)]NO3), and S-, N-, C-bound CH3Hg(II) (as in [(CH3Hg)3(6-MNuc)]NO3) have been prepared in aqueous solution at appropriate pH and mole ratios of the constituents. The complexes were characterized by means of 1H and 13C nmr and ir spectroscopy and elemental analysis. Formation of C-bound methylmercurated species extends our previous results obtained with xanthosine, inosine, and imidazole derivatives, and substantiates our proposal that activation through electrophilic coordination at N(7) is a requirement for C(8)—H abstraction. 2J(1H–199Hg) coupling constants, measured in (CD3)2SO for a number of CH3Hg(II) complexes of N-, S-, and C-donor heterocyclic ligands, including the 6-mercaptopurine riboside of the present study, correlate well with the 1J(13C–199Hg) coupling constants, according to 1J = 8.4602J − 155.6. The significance of this correlation in terms of the strength of the Hg–ligand bond is considered. The results could provide insight into the apparent selectivity of binding of CH3Hg(II) by bio-ligands, as well as in the design of chemotherapeutic agents for the treatment of methylmercury poisoning.

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