Related ArticlesThe hydrolysis of the anti-cancer ruthenium complex NAMI-A affects its DNA binding and antimetastatic activity: an NMR evaluation.
J Inorg Biochem. 2004 Feb;98(2):402-12
Authors: Bacac M, Hotze AC, van der Schilden K, Haasnoot JG, Pacor S, Alessio E, Sava G, Reedijk J
The coordination of the antimetastatic agent NAMI-A, [H(2)im][trans-RuCl(4)(dmso-S)(Him)], (Him=imidazole; dmso=dimethyl sulfoxide), to the DNA model base 9-methyladenine (9-MeAde) was investigated in water. NMR spectroscopy was first applied for the study of the molecular stability and hydrolysis of NAMI-A in aqueous solution over a range of pH (3.0-7.4) and chloride ion concentrations (0-1 M) at 37.0 degrees C. In physiological conditions (phosphate buffer, pH 7.4) NAMI-A disappears from the solution in 15 min due to chloride and dmso hydrolysis, leading to uncharacterised poly-oxo Ru species. Conversely, at lower pH (3.0-6.0) and in water (pH approximately 5.5), only a partial dmso hydrolysis occurs, slowly forming the [trans-RuCl(4)(H(2)O)(Him)](-) complex. This latter species coordinates to 9-MeAde (via the N7 of 9-MeAde), forming the [trans-RuCl(4)(9-MeAde)(Him)](-) complex. NAMI-A and [trans-RuCl(4)(H(2)O)(Him)](-) give comparable intracellular ruthenium concentrations and accumulate in KB cells (human mouth carcinoma) and accumulate these at the G(2)/M phase, while poly-oxo Ru species do not, and their cell uptake is reduced to 50%. On the contrary, G(2)/M arrest and protein content in the murine metastatic cell line metGM, are not influenced by NAMI-A hydrolysis. Hydrolysed NAMI-A species apparently are easier taken up by the metGM cells, showing intracellular ruthenium concentrations one order of magnitude greater than those of intact NAMI-A. Therefore, it is proposed that the selective antimetastatic activity of NAMI-A during in vivo experiments can be attributed to its hydrolysed species.
Ruthenium Agostic (Phosphinoaryl)borane Complexes: Multinuclear Solid-State and Solution NMR, X-ray, and DFT Studies
Ruthenium Agostic (Phosphinoaryl)borane Complexes: Multinuclear Solid-State and Solution NMR, X-ray, and DFT Studies
Yann Gloaguen, Gilles Alcaraz, Alban S. Petit, Eric Clot, Yannick Coppel, Laure Vendier and Sylviane Sabo-Etienne
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja203828r/aop/images/medium/ja-2011-03828r_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/ja203828r
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/extLacz2EPY
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Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Biochim Biophys Acta. 2011 Jan;1808(1):498-507
Authors: Mishra VK, Palgunachari MN, Hudson JS, Shin R, Keenum TD, Krishna NR, Anantharamaiah GM
The surprising observation that a 10-residue class G(?) peptide from apolipoprotein J, apoJ, possesses...
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A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
Chemistry. 2011 Feb 1;17(5):1547-1560
Authors: Enríquez-Navas PM, Marradi M, Padro D, Angulo J, Penadés S
The structural and affinity details of the interactions of synthetic oligomannosides, linear (di-, tri-, and tetra-) and branched (penta- and hepta-),...
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A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
Chemistry. 2011 Jan 5;
Authors: Enríquez-Navas PM, Marradi M, Padro D, Angulo J, Penadés S
The structural and affinity details of the interactions of synthetic oligomannosides, linear (di-, tri-, and tetra-) and branched (penta- and hepta-), with the broadly...
[NMR paper] NMR structure of an anti-gp120 antibody complex with a V3 peptide reveals a surface i
NMR structure of an anti-gp120 antibody complex with a V3 peptide reveals a surface important for co-receptor binding.
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Structure. 2000 Apr 15;8(4):385-95
Authors: Tugarinov V, Zvi A, Levy R, Hayek Y, Matsushita S, Anglister J
BACKGROUND: The protein 0.5beta is a potent strain-specific human immunodeficiency virus type 1 (HIV-1) neutralizing antibody raised against the entire envelope glycoprotein (gp120) of...
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[NMR paper] Nucleotide binding and GTP hydrolysis by the 21-kDa product of the c-H-ras gene as mo
Nucleotide binding and GTP hydrolysis by the 21-kDa product of the c-H-ras gene as monitored by proton-NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Nucleotide binding and GTP hydrolysis by the 21-kDa product of the c-H-ras gene as monitored by proton-NMR spectroscopy.
Eur J Biochem. 1993 Apr 15;213(2):781-8
Authors: Löw A, Sprinzl M, Limmer S
Proton-NMR signals in the downfield region (below approximately 10...
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[NMR paper] Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophil
Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophilus as monitored by proton NMR.
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Biochemistry. 1992 Mar 24;31(11):2970-7
Authors: Limmer S, Reiser CO, Schirmer NK, Grillenbeck NW, Sprinzl M
Proton NMR experiments of the GTP/GDP-binding protein EF-Tu from the extremely thermophilic bacterium Thermus thermophilus HB8 in H2O have been performed paying special attention to the...