Speciation of precious metal anti-cancer complexes by NMR spectroscopy.
Drug Discov Today Technol. 2015 Sep;16:7-15
Authors: Zou T, Sadler PJ
Abstract
Understanding the mechanism of action of anti-cancer agents is of paramount importance for drug development. NMR spectroscopy can provide insights into the kinetics and thermodynamics of the binding of metallodrugs to biomolecules. NMR is most sensitive for highly abundant I=1/2 nuclei with large magnetic moments. Polarization transfer can enhance NMR signals of insensitive nuclei at physiologically-relevant concentrations. This paper reviews NMR methods for speciation of precious metal anti-cancer complexes, including platinum-group and gold-based anti-cancer agents. Examples of NMR studies involving interactions with DNA and proteins in particular are highlighted.
PMID: 26547416 [PubMed - as supplied by publisher]
[NMR paper] High-Quality NMR Structure of Human Anti-Apoptotic Protein Domain Mcl-1(171-327) for Cancer Drug Design.
High-Quality NMR Structure of Human Anti-Apoptotic Protein Domain Mcl-1(171-327) for Cancer Drug Design.
Related Articles High-Quality NMR Structure of Human Anti-Apoptotic Protein Domain Mcl-1(171-327) for Cancer Drug Design.
PLoS One. 2014;9(5):e96521
Authors: Liu G, Poppe L, Aoki K, Yamane H, Lewis J, Szyperski T
Abstract
A high-quality NMR solution structure is presented for protein hMcl-1(171-327) which comprises residues 171-327 of the human anti-apoptotic protein Mcl-1 (hMcl-1). Since this construct contains the three...
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05-03-2014 10:42 PM
[NMR paper] Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR.
Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR.
Related Articles Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR.
J Vis Exp. 2013;(82)
Authors: Shoshan MS, Tshuva EY, Shalev DE
Abstract
Copper (I) binding by metallochaperone transport proteins prevents copper oxidation and release of the toxic ions that may participate in harmful redox reactions. The Cu (I) complex of the peptide model of a Cu (I) binding metallochaperone protein, which includes the...
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01-01-2014 03:05 PM
[NMR paper] Direct Measurement of the Mn(II) Hydration State in Metal Complexes and Metalloproteins Through 17O NMR Linewidths.
Direct Measurement of the Mn(II) Hydration State in Metal Complexes and Metalloproteins Through 17O NMR Linewidths.
Direct Measurement of the Mn(II) Hydration State in Metal Complexes and Metalloproteins Through 17O NMR Linewidths.
J Am Chem Soc. 2013 Oct 3;
Authors: Gale EM, Zhu J, Caravan P
Abstract
Here we describe a simple method to estimate the inner-sphere hydration state of the Mn(II) ion in coordination complexes and metalloproteins. The linewidth of bulk H217O is measured in the presence and absence of Mn(II) as a function...
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10-04-2013 05:23 PM
Can metal ion complexes be used as polarizing agents for solution DNP? A theoretical discussion
From The DNP-NMR Blog:
Can metal ion complexes be used as polarizing agents for solution DNP? A theoretical discussion
Luchinat, C., G. Parigi, and E. Ravera, Can metal ion complexes be used as polarizing agents for solution DNP? A theoretical discussion. J. Biomol. NMR, 2013: p. 1-11.
http://www.ncbi.nlm.nih.gov/pubmed/23606273
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06-03-2013 04:21 PM
[NMR paper] Determination of the electron relaxation rates in paramagnetic metal complexes: appli
Determination of the electron relaxation rates in paramagnetic metal complexes: applicability of available NMR methods.
Related Articles Determination of the electron relaxation rates in paramagnetic metal complexes: applicability of available NMR methods.
J Magn Reson. 2004 Apr;167(2):169-77
Authors: Jensen MR, Led JJ
Four different approaches for determining the electron relaxation rates in paramagnetic metallo-proteins are investigated, using a paramagnetic Ni2+ complex of a protein as an example. All four approaches rely on the...
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11-24-2010 09:51 PM
[NMR paper] The hydrolysis of the anti-cancer ruthenium complex NAMI-A affects its DNA binding an
The hydrolysis of the anti-cancer ruthenium complex NAMI-A affects its DNA binding and antimetastatic activity: an NMR evaluation.
Related Articles The 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, , (Him=imidazole; dmso=dimethyl sulfoxide), to the DNA model base...
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11-24-2010 09:25 PM
[NMR paper] Metal complexes as allosteric effectors of human hemoglobin: an NMR study of the inte
Metal complexes as allosteric effectors of human hemoglobin: an NMR study of the interaction of the gadolinium(III) bis(m-boroxyphenylamide)diethylenetriaminepentaacetic acid complex with human oxygenated and deoxygenated hemoglobin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Metal complexes as allosteric effectors of human hemoglobin: an NMR study of the interaction of the...
Speciation of precious metal anti-cancer complexes by NMR spectroscopy.
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