Source:http://linkedlifedata.com/resource/pubmed/id/19290551
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
|
pubmed:dateCreated |
2009-7-28
|
pubmed:abstractText |
A series of oxovanadium complexes with mixed ligands, a tridentate ONO-donor Schiff base ligand [viz., salicylidene anthranilic acid (SAA)], and a bidentate NN ligand [viz., 2,2'-bipyridine (bpy), 1,10-phenanthroline (phen), dipyrido[3,2-d:2',3'-f]quinoxaline (dpq), dipyrido[3,2-a:2',3'-c]phenazine (dppz), or 7-methyldipyrido[3,2-a:2',3'-c]phenazine (dppm)], have been synthesized and characterized by elemental analysis, electrospray ionization mass spectrometry, UV-vis spectroscopy, Fourier transform IR spectroscopy, EPR spectroscopy, and X-ray crystallography. Crystal structures of both complexes, [V(IV)O(SAA)(bpy)].0.25bpy and [V(IV)O(SAA)(phen)].0.33H(2)O, reveal that oxovanadium(IV) is coordinated with one nitrogen and two oxygen atoms from the Schiff base and two nitrogen atoms from the bidentate planar ligands, in a distorted octahedral geometry (VO(3)N(3)). The oxidation state of V(IV) with d(1) configuration was confirmed by EPR spectroscopy. The speciation of VO-SAA-bpy in aqueous solution was investigated by potentiomtreic pH titrations, and the results revealed that the main species are two ternary complexes at a pH range of 7.0-7.4, and one is the isolated crystalline complex. The complexes have been found to be potent inhibitors against human protein tyrosine phosphatase 1B (PTP1B) (IC(50) approximately 30-61 nM), T-cell protein tyrosine phosphatase (TCPTP), and Src homology phosphatase 1 (SHP-1) in vitro. Interestingly, the [V(IV)O(SAA)(bpy)] complex selectively inhibits PTP1B over the other two phosphatases (approximate ninefold selectivity against SHP-1 and about twofold selectivity against TCPTP). Kinetics assays suggest that the complexes inhibit PTP1B in a competitive and reversible manner. These suggest that the complexes may be promising candidates as novel antidiabetic agents.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Organometallic Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Pyridines,
http://linkedlifedata.com/resource/pubmed/chemical/Schiff Bases,
http://linkedlifedata.com/resource/pubmed/chemical/Vanadium
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
1432-1327
|
pubmed:author | |
pubmed:issnType |
Electronic
|
pubmed:volume |
14
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
841-51
|
pubmed:meshHeading |
pubmed-meshheading:19290551-Absorption,
pubmed-meshheading:19290551-Electrons,
pubmed-meshheading:19290551-Enzyme Inhibitors,
pubmed-meshheading:19290551-Humans,
pubmed-meshheading:19290551-Kinetics,
pubmed-meshheading:19290551-Ligands,
pubmed-meshheading:19290551-Microscopy, Energy-Filtering Transmission Electron,
pubmed-meshheading:19290551-Organometallic Compounds,
pubmed-meshheading:19290551-Potentiometry,
pubmed-meshheading:19290551-Protein Tyrosine Phosphatases,
pubmed-meshheading:19290551-Pyridines,
pubmed-meshheading:19290551-Schiff Bases,
pubmed-meshheading:19290551-Spectrometry, Mass, Electrospray Ionization,
pubmed-meshheading:19290551-Vanadium
|
pubmed:year |
2009
|
pubmed:articleTitle |
Ternary oxovanadium(IV) complexes of ONO-donor Schiff base and polypyridyl derivatives as protein tyrosine phosphatase inhibitors: synthesis, characterization, and biological activities.
|
pubmed:affiliation |
Institute of Molecular Science, The Key Laboratory of Chemical Biology and Molecular Engineering of Education Ministry, Shanxi University, Taiyuan, China.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|