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Crystal structure of diethyl [(4-nitro-phenyl-amino)(2-hy-droxy-phen-yl)meth-yl]phospho-nate methanol monosolvate.
Acta Crystallogr Sect E Struct Rep Online
PUBLISHED: 09-01-2014
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In the title compound, C17H21N2O6P·CH3OH, the planes of the 4-nitro-aniline and 2-hy-droxy-phenyl groups form a dihedral angle of 84.04?(8)°. The P atom exhibits tetra-hedral geometry involving two O-ethyl groups, a C? atom and a double-bonded O atom. In the crystal, O-H?O, N-H?O and C-H?O hydrogen bonds link the ?-amino-phospho-nic acid and methanol mol-ecules into chains that propagate parallel to the a axis.
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Protein tyrosine phosphatase inhibition by metals and metal complexes.
Antioxid. Redox Signal.
PUBLISHED: 02-19-2014
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Protein tyrosine phosphatases (PTPs) play essential roles in controlling cell proliferation, differentiation, communication, and adhesion. The dysregulated activities of PTPs are involved in the pathogenesis of a number of human diseases such as cancer, diabetes, and autoimmune diseases.
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Potent and selective inhibition of T-cell protein tyrosine phosphatase (TCPTP) by a dinuclear copper(II) complex.
Chem. Commun. (Camb.)
PUBLISHED: 12-12-2011
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A dinuclear Cu(II) complex, [Cu(2)(?-IDA)(phen)(3)(NO(3))]NO(3)·4H(2)O (phen = 1,10-phenanthroline, H(2)IDA = iminodiacetic acid), was found to potently and selectively inhibit T-cell protein tyrosine phosphatase, and lead to the anti-proliferation and apoptosis of C6 glioma cells.
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Potent inhibition of protein tyrosine phosphatases by quinquedentate binuclear copper complexes: synthesis, characterization and biological activities.
Dalton Trans
PUBLISHED: 10-25-2011
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Three phosphono-containing multidentate ligands were employed to synthesize quinquedentate binuclear copper complexes, [Cu(2)L(2)] (1-3) (H(2)L1 = diethyl(propane-1,3-diylbis(azanediyl))bis((2-hydroxyphenyl)methylene)bis(hydrogen phosphonate), H(2)L2 = diethyl(ethane-1,2-diylbis(azanediyl))bis((2-hydroxyphenyl)methylene)bis(hydrogen phosphonate), H(2)L3 = diethyl(hexane-1,6-diylbis(azanediyl))bis((2-hydroxyphenyl)methylene)bis(hydrogen phosphonate)), which were characterized by elemental analysis, IR, X-ray diffraction analysis, electrospray ionization mass spectra. Complexes 1 and 2 crystallized in the triclinic system with space group P ?1. The speciation of the Cu-H(2)L1 system in aqueous solution was investigated by potentiometric pH titrations. The three dicopper complexes exhibited potent and almost the same inhibitory effects against protein tyrosine phosphatase 1B (PTP1B) and T-cell protein tyrosine phosphatase (TCPTP) with IC(50) of 0.16-0.24 ?M, about 10-fold stronger inhibition than against Src homology phosphatase 1 (SHP-1), 30-fold than against Src homology phosphatase 2 (SHP-2) and more than 100-fold than against megakaryocyte protein-tyrosine phosphatase 2 (PTP-MEG2). Fluorescence titrations revealed complex 1 bond to the five PTPs with molar ratio of 1:1 and binding constants of 1.62 × 10(6), 3.09 × 10(6), 1.95 × 10(5), 2.24 × 10(5), 1.55 × 10(4) M(-1) for PTP1B, TCPTP, SHP-1, SHP-2 and PTP-MEG2, respectively, consistent with the inhibitory abilities from IC(50) and K(i) values. Also, the three copper complexes could inhibit phosphatase activity of cell extracts from C6 rat glioma cells. The results suggested the structures of copper complexes influence selectivity over different PTPs.
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Mononuclear copper(II) complexes with 3,5-substituted-4-salicylidene-amino-3,5-dimethyl-1,2,4-triazole: synthesis, structure and potent inhibition of protein tyrosine phosphatases.
Dalton Trans
PUBLISHED: 05-24-2011
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Six copper complexes of Schiff base ligands containing 3,5-substituted-4-salicylideneamino-3,5-dimethyl-1,2,4-triazole have been synthesized and well characterized. The structures of complexes 1 and 2 were determined by X-ray crystal analysis. Fluorescence and potentiometric study indicated that in the physiological pH range, one ligand was dissociated from the complexes to form 1:1 mononucleus copper complexes. The complexes potently inhibit protein tyrosine phosphatase 1B (PTP1B), T-cell protein tyrosine phosphatase (TCPTP), megakaryocyte protein tyrosine phosphatase 2 (PTP-MEG2) and Src homology phosphatase 1 (SHP-1) with 3-4 fold selectivity against PTP1B over TCPTP and PTP-MEG2, and 3-9 fold over SHP-1, but display almost no inhibition against Src homology phosphatase 2 (SHP-2). Complex 1 inhibits PTP1B with a competitive model with K(i) of 30 nM. Substitution with small groups at the phenyl of the ligand does not obviously influence the inhibitory ability of the complexes.
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2-(4-Methyl-phen-yl)-1H-imidazo[4,5-f][1,10]phenanthroline.
Acta Crystallogr Sect E Struct Rep Online
PUBLISHED: 03-05-2011
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In the title compound, C(20)H(14)N(4), all the non-H atoms are roughly coplanar with an r.m.s. deviation of 0.0776?Å. In the crystal, mol-ecules are linked by N-H?N hydrogen bonds, forming chains along the ([Formula: see text]). The chains are connected by inter-molecular C-H?N hydrogen bonds and ?-? stacking inter-actions between inversion-related phenanthroline, imidazole and phenyl rings with centroid-centroid distances in the range 3.777?(1)-3.905?(1)?Å.
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Ternary oxovanadium(IV) complexes with amino acid-Schiff base and polypyridyl derivatives: synthesis, characterization, and protein tyrosine phosphatase 1B inhibition.
J. Inorg. Biochem.
PUBLISHED: 02-22-2011
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To investigate the structure-activity relationship of vanadium complexes in inhibiting protein tyrosine phosphatase1B (PTP1B), eight mixed-ligand oxovanadium(IV) complexes, [V(IV)O(SalAla)(NN)] (H(2)SalAla for salicylidene alanine, NN for N,N-donor heterocyclic base, namely, 2,2-bipyridine (bpy, 1), 1,10-phenanthroline (phen, 2), dipyrido[3,2-d:2,3-f]quinoxaline (dpq, 3), dipyrido[3,2-a:2,3-c]phenazine (dppz, 4)), [V(IV)O(SalLys)(dpq)] (5), [V(IV)O(SalLys)(dppz)] (6), [V(IV)O(SalAsp)(dppz)], (7) and [V(IV)O(SalTrp)(dppz)] (8)), of which 3-8 are new, have been prepared and characterized by elemental analysis, infrared, UV-visible, electrospray ionization mass spectrometry and conductivity. The molar conductance data confirmed the non-electrolytic nature of the complexes in DMSO solution. The coordination in [V(IV)O (SalAla)(phen)] (2) was confirmed by X-ray crystal structure analysis. The oxidation state of V(IV) with d(1) configuration in 2 was confirmed by EPR. The speciation of VO-SalAla-phen in aqueous solution was investigated by potentiometric pH titrations. The results indicate that the main species are two ternary complexes at the pH range 7.0-7.4. Biochemical assays demonstrate that the mixed-ligand oxovanadium(IV) complexes are potent inhibitors of PTP1B with IC(50) values in the range of 62-597nM, approximately 3-10 fold weaker in potency than those of similar mixed-ligand oxovanadium(IV) complexes of salicylidene anthranilic acid (SAA) derivative with polypyridyl ligands, except complex 8, which exhibits comparable or better inhibition activity than those of the mixed-ligand oxovanadium(IV) complexes of SAA derivative with polypyridyl ligands. The results demonstrate that the structures of vanadium complexes influence the PTP1B inhibition activity. Kinetics assays reveal that complex 2 inhibits PTP1B in a competitive manner.
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Metal-based inhibitors of protein tyrosine phosphatases.
Anticancer Agents Med Chem
PUBLISHED: 02-05-2011
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Protein tyrosine phosphatases (PTPs) are a large family of signaling enzymes playing critical role in signal transduction and regulation of cellular processes. Dysfunction of PTP activity is associated with diabetes, cancer, autoimmune disorders, and neural diseases. PTP inhibitors therefore emerged as promising therapeutic targets. Recent research indicates that besides small organic molecules, metal ions and metal complexes can also strongly inhibit PTPs both in vitro and in vivo, resulting in the increase of phosphorylation of corresponding substrates and the modulation of cellular process. Structure of metal complexes influences the potency and selectivity of PTP inhibition. Detailed studies on this subject are not only expected to yield metal-based drugs targeting individual PTPs, but also to support understanding the function of metals in organisms. This review focuses on recent advancements in this area of research.
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Dinuclear copper complexes of organic claw: potent inhibition of protein tyrosine phosphatases.
J. Inorg. Biochem.
PUBLISHED: 01-21-2011
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Three dinuclear copper complexes of organic claw ligands (2,2,2?,2-(5-R-2-hydroxy-1,3-phenylene)bis(methylene)bis(azanetriyl)tetraacetic acid, R=methyl (H(5)L1), chloro (H(5)L2) and bromo (H(5)L3)): [Cu(2)NaL1(H(2)O)(2)] (1), [Cu(2)HL2(H(2)O)(2)] (2), [Cu(2)NaL3(H(2)O)(2)] (3), have been synthesized and characterized by elemental analyses, infrared spectra, thermo-gravimetric analyses, X-ray diffraction analysis, electrospray ionization mass spectra, pH-potentiometric titration, molar conductivity. Their inhibitory effects against human protein tyrosine phosphatase 1B (PTP1B), T cell protein tyrosine phosphatase (TCPTP), Megakaryocyte protein tyrosinephosphatase 2 (PTP-MEG2), srchomology phosphatase 1 (SHP-1) and srchomology phosphatase 2 (SHP-2) are evaluated in vitro. The three copper complexes exhibit potent and almost same inhibition against PTP1B and SHP-1 with IC(50) values ranging from 0.15 to 0.31?M, about 2-fold stronger inhibition than against PTP-MEG2, 10-fold stronger inhibition than against TCPTP, but almost no inhibition against SHP-2. Kinetic analysis indicates that they are reversible competitive inhibitors of PTP1B. Molecular docking analyses confirm the inhibition model. Fluorescence titration studies suggest that the complexes bond to PTP1B with the formation of a 1:1 complex. The results demonstrate that copper complexes that are potent PTPs inhibitors but have different inhibitory effects over different PTPs, may be explored as new practical inhibitors towards individual PTP with some specificity.
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Potent inhibition of protein tyrosine phosphatases by copper complexes with multi-benzimidazole derivatives.
Biometals
PUBLISHED: 01-07-2011
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A series of copper complexes with multi-benzimidazole derivatives, including mono- and di-nuclear, were synthesized and characterized by Fourier transform IR spectroscopy, UV-Vis spectroscopy, elemental analysis, electrospray ionization mass spectrometry. The speciation of Cu/NTB in aqueous solution was investigated by potentiometric pH titrations. Their inhibitory effects against human protein tyrosine phosphatase 1B (PTP1B), T-cell protein tyrosine phosphatase (TCPTP), megakaryocyte protein tyrosine phosphatase 2 (PTP-MEG2), srchomology phosphatase 1 (SHP-1) and srchomology phosphatase 2 (SHP-2) were evaluated in vitro. The five copper complexes exhibit potent inhibition against PTP1B, TCPTP and PTP-MEG2 with almost same inhibitory effects with IC(50) at submicro molar level and about tenfold weaker inhibition versus SHP-1, but almost no inhibition against SHP-2. Kinetic analysis indicates that they are reversible competitive inhibitors of PTP1B. Fluorescence study on the interaction between PTP1B and complex 2 or 4 suggests that the complexes bind to PTP1B with the formation of a 1:1 complex. The binding constant are about 1.14 × 10(6) and 1.87 × 10(6) M(-1) at 310 K for 2 and 4, respectively.
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A highly selective OFF-ON fluorescent sensor for zinc in aqueous solution and living cells.
Chem. Commun. (Camb.)
PUBLISHED: 10-06-2010
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A novel compound, 2-p-tolyl-1H-imidazo[4,5-f][1,10]phenanthrolinium hydrogenselenite (HMPIP·HSeO(3), C1), shows a peculiar OFF-ON fluorescent response to Zn(2+) in aqueous solution and living cells.
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Synthesis and characterisation of Mn(II), Co(II) and Cd(II) coordination polymers of 1,2,4-triazole-3, 5-dicarboxylic acid.
Dalton Trans
PUBLISHED: 05-26-2010
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Three new coordination polymers ([Mn(3)(dctrz)(2)(H(2)O)(8)](n) (1), [Co(Hdctrz)(H(2)O)(3)](n) (2) and [Cd(Hdctrz)(H(2)O)(2)](n) (3), H(3)dctrz, 1-H-1,2,4-triazole-3,5-dicarboxylic acid) based on the self-assembly of Mn(2+), Co(2+) and Cd(2+) ions with H(3)dctrz have been synthesized and characterized by single crystal X-ray diffraction analysis. Variable temperature magnetic studies are investigated for complexes 1 and 2. Complex 1 is assembled into a one-dimensional molecular chain via trinuclear units formed from two dctrz anion bridges and eight coordination waters. In 2, the central Co(2+) cations with six-coordinated octahedron geometry are bridged by Hdctrz anions to form one-dimensional zigzag chain structures. Complex 3 displays a 2D rhombus grid-like architecture with a (4, 4) topology, achieved through Hdctrz anion bridges. Both complexes 1 and 2 exhibit S = 5/2 (Mn(2+)) and S = 3/2 (Co(2+)) spin Heisenberg chains with alternating and regular magnetic sequences. Variable temperature (1.8-300 K) magnetic studies indicate weak antiferromagnetic coupling between the metal centres in complexes 1 and 2.
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Potent inhibition of protein tyrosine phosphatase 1B by copper complexes: implications for copper toxicity in biological systems.
Chem. Commun. (Camb.)
PUBLISHED: 04-09-2010
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A new dinuclear copper complex and several Cu-amino acid complexes inhibit protein tyrosine phosphatase 1B competitively at submicromolar levels, suggesting that copper complexes may interfere with cellular signaling pathways by inhibiting protein tyrosine phosphatases.
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Synthesis, characterization, and protein tyrosine phosphatases inhibition activities of oxovanadium(IV) complexes with Schiff base and polypyridyl derivatives.
J. Inorg. Biochem.
PUBLISHED: 02-17-2010
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Seven new mixed-ligand vanadyl complexes, [V(IV)O(5-Br-SAA)(NN)] and [V(IV)O(2-OH-NAA)(NN)] (1-7) (5-Br-SAA for 5-bromosalicylidene anthranilic acid, 2-OH-NAA for 2-hydroxy-1-naphthaldehyde anthranilic acid and NN for N,N-donor heterocyclic base, namely, 2,2-bipyridine (bpy, 1 and 5), 1,10-phenanthroline (phen, 2 and 6), dipyrido[3,2-d:2,3-f]quinoxaline (dpq, 3 and 7), dipyrido[3,2-a:2,3-c]phenazine (dppz, 4)), were synthesized and characterized. X-ray crystal structure of [V(IV)O(5-Br-SAA)(phen)] revealed a distorted octahedral geometry with the Schiff base ligand coordinated in a tridentate ONO-fashion and the phenanthroline ligand in a bidentate fashion. Density-functional theory (DFT) calculations suggest a similar structure and the same coordination mode for all the other oxovanadium complexes synthesized. Biochemical assays demonstrate that the mixed-ligand oxovanadium(IV) complexes are potent inhibitors of protein tyrosine phosphatase 1B (PTP1B), with IC(50) values approximately 41-75 nM. Kinetics assays suggest that the complexes inhibit PTP1B in a competitive manner. Notably, they had moderate selectivity of PTP1B over T-cell protein tyrosine phosphatase (TCPTP) (about 2-fold) and good selectivity over Src homology phosphatase 1 (SHP-1) (about 4 approximately 7-fold). Thus, these mixed-ligand complexes represent a promising class of PTP1B inhibitors for future development as anti-diabetic agents.
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Inhibition protein tyrosine phosphatases by an oxovanadium glutamate complex, Na2[VO(Glu)2(CH3OH)](Glu = glutamate).
Biometals
PUBLISHED: 01-18-2010
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The insulin-sensitizing effect of vanadium complexes has been linked to their ability to inhibit protein tyrosine phosphatases (PTPs). Considering that vanadium complexes may exchange in vivo with amino acids, forming in situ vanadium-amino acid complexes, we have synthesized and characterized an oxovanadium glutamate complex, Na(2)[V(IV)O(Glu)(2)(CH(3)OH)]H(2)O (1·H(2)O). The complex showed potent inhibition against four human PTPs (PTP1B, TCPTP, HePTP, and SHP-1) with IC(50) in the 0.21-0.37 ?M ranges. Fluorescence titration studies suggest that the complex binds to PTP1B with the formation of a 2:1 complex. Enzyme kinetics analysis using Lineweaver-Burk plots indicates a typical competitive inhibition mode.
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Rationally designed chiral Ni5L6 clusters with the in situ generated tridentate ligand. Hydrothermal synthesis, crystal structures, morphology and magnetic properties.
Dalton Trans
PUBLISHED: 06-29-2009
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A series of rationally designed pentanuclear clusters with D(3) symmetry have been synthesized and structurally characterized. The complexes were of formula [Ni(5)L(6)]X(n)Y(4-n) x mH(2)O [2-4, X = NO(3), Y = OH, n = 1, m = 3 (5); X = Br, n = 4, m= 4 (6); X = I, n = 4, m= 0 (7)], where the ligand [L, (Z)-1,2-di(1H-benzoimidazol-2-yl)ethenol] was produced in situ under hydrothermal conditions. SEM images proved that the crystals of compounds 2-4, 6 and 7 were hollow tetragonal or hexagonal prisms, and a nucleation-dissolution-recrystallization mechanism was investigated. Complexes 3 and 4 demonstrated chirality from CD spectra. Magnetic susceptibility measurements of 4-7 showed the occurrence of antiferromagnetic interactions, and the all negative J values fitted of the variable-temperature magnetic susceptibility data applying the spin matrix method confirmed the overall antiferromagnetic exchange in the clusters.
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Ternary oxovanadium(IV) complexes of ONO-donor Schiff base and polypyridyl derivatives as protein tyrosine phosphatase inhibitors: synthesis, characterization, and biological activities.
J. Biol. Inorg. Chem.
PUBLISHED: 03-04-2009
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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.
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Hexakis(2-amino-pyridinium) di-?(6)-oxido-tetra-?(3)-oxido-tetra-deca-?(2)-oxido-octa-oxidodeca-vanadium(V) dihydrate.
Acta Crystallogr Sect E Struct Rep Online
PUBLISHED: 01-12-2009
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In the title compound, (C(5)H(7)N(2))(6)[V(10)O(28)]·2H(2)O, the [V(10)O(28)](6-) anion is generated by crystallographic inversion symmetry and each of the five vanadium centres adopts a distorted VO(6) octa-hedral geometry. In the crystal structure, a network of N-H?O, N-H?(O,O) and O-H?O hydrogen bonds helps to establish the packing.
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Synthesis and evaluation of oxovanadium(IV) complexes of Schiff-base condensates from 5-substituted-2-hydroxybenzaldehyde and 2-substituted-benzenamine as selective inhibitors of protein tyrosine phosphatase 1B.
Dalton Trans
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Five oxovanadium(IV) complexes, which were divided into two groups, [V(IV)O(bhbb, nhbb)(H(2)O)(2)] (tridentate ligands: H(2)bhbb = 2-(5-bromo-2-hydroxylbenzylideneamino)benzoic acid, 1; H(2)nhbb = 2-(5-nitro-2-hydroxylbenzylideneamino)benzoic acid, 2) and [V(IV)O(cpmp, bpmp, npmp)(2)] (bidentate ligands: Hcpmp = 4-chloro-2-((phenylimino)methyl)phenol, 3; Hbpmp = 4-bromo-2-((phenylimino)methyl)phenol, 4; Hnpmp = 4-nitro-2-((phenylimino)methyl) phenol, 5) have been prepared and characterized by elemental analysis, infrared, UV-visible and electrospray ionization mass spectrometry. The coordination in [V(IV)O(bhbb)(H(2)O)(2)] (1) was confirmed by X-ray crystal structure analysis. The oxidation state of V(IV) with d(1) configuration in 1-5 was confirmed by EPR. The speciation of VO/H(2)bhbb in methanol-aqueous solution was investigated by potentiometric pH titrations. The result indicated that the main species were [V(IV)O(bhbb)(OH)](-) and [V(IV)O(bhbb)(OH)(2)](2-) at the pH range 7.0-7.4. The structure-activity relationship of the vanadium complexes in inhibiting protein tyrosine phosphatases (protein tyrosine phosphatase 1B, PTP1B; T-cell protein tyrosine phosphatase, TCPTP; megakaryocyte protein-tyrosine phosphatase, PTP-MEG2; Src homology phosphatase 1, SHP-1 and Src homology phosphatase 2, SHP-2) was investigated. The oxovanadium(IV) complexes were potent inhibitors of PTP1B, TCPTP, PTP-MEG2, SHP-1 and SHP-2, but exhibited different inhibitory abilities over different PTPs. Complexes 2 and 4 displayed better selectivity to PTP1B over the other four PTPs. Kinetic data showed that complex 2 inhibited PTP1B, TCPTP and SHP-1 with a noncompetitive inhibition mode, but a classical competitive inhibition mode for PTP-MEG2 and SHP-2. The results demonstrated that both the structures of vanadium complexes and the conformations of PTPs influenced PTP inhibition activity. The proper modification of the organic ligand moieties may result in screening potent and selective vanadium-based PTP1B inhibitors.
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2,2,2,2-(1,4-Phenyl-enedinitrilo)-tetra-acetic acid dihydrate.
Acta Crystallogr Sect E Struct Rep Online
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In the title compound, C(14)H(16)N(2)O(8)·2H(2)O, the complete organic molecule is generated by crystallographic inversion symmetry. The dihedral angles between the aniline ring and the acetic acid groups are almost identical, viz. 82.61?(7) and 80.33?(7)°. In the crystal, O-H?O hydrogen bonds link the organic mol-ecules and water mol-ecules, forming zigzag chains the c axis. An intra-molecular O-H?O hydrogen bond is also observed.
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Exploration of biguanido-oxovanadium complexes as potent and selective inhibitors of protein tyrosine phosphatases.
Biometals
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The inhibitory effects of three biguanido-oxovanadium complexes ([VO(L(1-3))(2)]·nH(2)O: HL(1) = metformin, HL(2) = phenformin, HL(3) = moroxydine) against four protein tyrosine phosphatases (PTPs) and an alkaline phosphatase (ALP) were investigated. The complexes display strong inhibition against PTP1B and TCPTP (IC(50), 80-160 nM), a bit weaker inhibition against HePTP (IC(50), 190-410 nM) and SHP-1(IC(50), 0.8-3.3 ?M) and much weaker inhibition against ALP (IC(50), 17-35 ?M). Complex 3 is about twofold less potent against PTP1B, TCPTP and HePTP than complexes 1 and 2, while complex 2 inhibits SHP-1 more strongly (about three to fourfold) than the other two complexes. These results suggest that the structures of the ligands slightly influence the potency and selectivity against PTPs. The complexes inhibit PTP1B and ALP with a typical competitive type.
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Exploration of ?-aminophosphonate N-derivatives as novel, potent and selective inhibitors of protein tyrosine phosphatases.
Eur J Med Chem
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Seventeen ?-aminophosphonates are synthesized. Their compositions and structures are established by EA, UV, FT-IR, (1)H NMR, (13)C NMR, (31)P NMR and ESI-MS. Compounds 1-4 are confirmed by X-ray crystallography. PTP inhibition shows compounds 1-5, 12, 15 are moderate competitive inhibitors with some selectivity. The most potent inhibitor is compound 5 with the lowest IC(50) value about 6.64 ?M against PTP1B, about 2-fold and 25-fold stronger than against TCPTP and PTP-MEG2 while it doesnt inhibit SHP-1 and SHP-2. The binding constant of 5 to PTP1B is 2.23 × 10(5) M(-1) and binding ratio approximates 1:1. Cell viability and apoptosis assays indicate 5 is cell permeable with lower cytotoxicity. The results indicate ?-aminophosphonates are possibly developed to effective and selective inhibitors of PTPs.
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