Dinuclear copper complexes of organic claw: Potent inhibition of protein tyrosine phosphatases

Ma, Ling; Lü, Liping; Zhu, Mei; Wang, Qing-Ming; Gao, Fei; Yuan, Caixia; Wu, Yanbo; Xing, Shu; Fu, Xueqi; Mei, Yuhua; Gao, Xiaoli

doi:10.1016/j.jinorgbio.2011.05.015

Cited by 22 publications

(9 citation statements)

References 47 publications

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“…It is different from dinuclear copper complexes of organic claw ligands which exhibit potent and almost the same inhibition against PTP1B and SHP-1 with IC 50 values ranging from 0.15 to 0.31 lM, about Fig. 1 The structure of complexes 1-5 twofold weaker inhibition against PTP-MEG2, tenfold weaker inhibition against TCPTP (Ma et al 2011a), and copper complexes of Schiff base ligands containing 3,5-substituted-4-salicylideneamino-3,5-dimethyl-1,2,4-triazole which strongly inhibit PTP1B with IC 50 from 0.038 to 0.091 lM, three-to fourfold selectivity against PTP1B over TCPTP and PTP-MEG2, and three-to ninefold over SHP-1 (Ma et al 2011b). It is interesting that these three types of copper complexes do not inhibit SHP-2.…”

Section: Ptp Inhibition Studiesmentioning

confidence: 88%

Potent inhibition of protein tyrosine phosphatases by copper complexes with multi-benzimidazole derivatives

et al. 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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Section: Ptp Inhibition Studiesmentioning

confidence: 88%

Potent inhibition of protein tyrosine phosphatases by copper complexes with multi-benzimidazole derivatives

et al. 2011

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“…Binuclear copper complexes with phosphono-containing multidentate ligands 23-25 display similar inhibition against PTP1B and TCPTP, with IC 50 values ranging from 0.15 to 0.24 lM, *10-, 30-, and more than 100-fold stronger inhibition than their inhibition of SHP-1, SHP-2, and PTP-MEG2 (111). The dinuclear copper complexes with organic claw ligands 26-28 exhibit almost the same inhibition of PTP1B and SHP-1, with IC 50 values in a range of 0.15-0.31 lM, *2-fold stronger inhibition than their inhibition of PTP-MEG2 and 10-fold stronger than their inhibition of TCPTP (66). Although the copper complexes with multibenzimidazoles 29-33 have almost the same inhibitory effects on PTP1B, TCPTP, and PTP-MEG2, with IC 50 values from 0.12 to 0.25 lM, they display about a 10-fold weaker inhibition of SHP-1 (61).…”

Section: Copper Complexesmentioning

confidence: 95%

Protein Tyrosine Phosphatase Inhibition by Metals and Metal Complexes

Lü

Zhu

2014

Antioxidants & Redox Signaling

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“…1 H NMR (400 MHz, DMSO-d6): δ 6.81 (s, 0H), 6.59 (s, 0H), 3.75 (s, 1H), 3.38 (s, 1H), 2.10 (s, 1H), 2.07 (s, 1H). 13 The catalyst BBTA was synthesized by modification of previous published procedures [44,45] as follows: NaOH (10 g) was added to 140 mL aqueous solution containing iminodiacetic acid (0.125 mol) and p-cresol (0.063 mol) under ice water bath. Then paraformaldehyde (0.063 mol) was added slowly into the mixture and the solution was stirred for 30 min at room temperature.…”

Section: Synthesismentioning

confidence: 99%

Highly Selective Isomerization of Glucose into Fructose Catalyzed by a Mimic Glucose Isomerase

Zhang

Meng

et al. 2019

ChemCatChem

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An amphoteric phenolic compound with carboxyl and amino functional groups was synthesized and used as mimic glucose isomerase to catalyze the isomerization of glucose into fructose. The mimic enzyme displayed excellent catalytic activity for isomerization of glucose to fructose under mild conditions. The yield of fructose and selectivity of fructose could reach 33.0 % and 93.5 % after reacting 4 h, respectively, at pH 8.5 and 80°C. The catalysis reaction rate constant k cat and Michaelis constants K mG , K mF were calculated. The activation energy of glucose to fructose was evaluated as 65.9 kJ mol À 1 . The possible catalysis reaction mechanism was proposed. The acid-base groups on the catalyst play an important role in proton extraction and transfer, as well as in the rotation of local carbon chain, which leads to the highly selective isomerization of glucose into fructose under mild conditions.

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Dinuclear copper complexes of organic claw: Potent inhibition of protein tyrosine phosphatases

Cited by 22 publications

References 47 publications

Potent inhibition of protein tyrosine phosphatases by copper complexes with multi-benzimidazole derivatives

Potent inhibition of protein tyrosine phosphatases by copper complexes with multi-benzimidazole derivatives

Protein Tyrosine Phosphatase Inhibition by Metals and Metal Complexes

Highly Selective Isomerization of Glucose into Fructose Catalyzed by a Mimic Glucose Isomerase

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