5706-80-9Relevant articles and documents
Efficient reduction of graphene oxide to graphene nanosheets using a silica-based ionic liquid: Synthesis, characterization and catalytic properties of IMD-Si/FeCl4-@GNS
Khan, Mohd Umar,Siddiqui, Shaheen,Khan, Waqas Ahmad,Siddiqui, Zeba N.
, p. 4822 - 4833 (2020)
The aim of the present protocol is to develop a facile route for the synthesis of novel ionic liquid (IL)-functionalized graphene nano sheets (IMD-Si/FeCl4-@GNS). An imidazolium IL with tetrachloroferrate as an anion (IMD-Si/FeCl4-) was used to reduce graphene oxide. IMD-Si/FeCl4-@GNS were well characterized using various techniques such as Fourier transform infrared (FTIR), Raman, ultraviolet-visible diffuse reflectance spectroscopy (UV-VIS DRS), scanning electron microscopy/energy dispersive X-ray (SEM/EDX), elemental mapping, transmission electron microscopy (TEM), powder X-ray diffraction (XRD), thermal gravimetry (TG), electron paramagnetic resonance (EPR), and X-ray photoelectron spectroscopy (XPS) analyses. The IL-functionalized material was investigated for its catalytic properties and found to be an efficient catalyst for the synthesis of (E)-selective substituted thiosemicarbazone derivatives. The (E)-selectivity was confirmed using DFT calculations which showed that the (E)-isomer was stabilized by 4.90 kcal mol-1 more than the (Z)-isomer. The catalyst maintained its catalytic activity for six successive runs.
Synthesis and crystal structure of [chlorobis(triphenylphospino)(p-chlorobenzaldehyde thiosemicarbazone)] copper(I) complex
Khan, Ashiq,Sharma, Poonam,Rajnikant,Gupta, Vivek K.,Padha, Naresh,Sharma, Rekha
, p. 185 - 191 (2016)
Reactions of copper(I) halides with p-chlorobenzaldehyde thiosemicarbazone (H1L) and triphenylphosphine in 1: 1: 2 molar ratio yielded complexes of stoichiometry, [CuX(η 1-S- H 1L)(Ph3P)2] (X = I, 1: Br, 2; Cl, 3). All the three complexes were characterized using analytical (CHNS) and spectroscopic (IR, 1H NMR) techniques. The structure of complex 3 was confirmed by X-ray crystallography. It has been found to crystallize in the triclinic system with space group P-1 and unit cell parameters: a = 10.207(5) ?, b = 13.027(5) ?, c = 16.269(5) ?, α= 100.054(5), β= 99.228(5) and γ= 97.234(5). This complex has distorted tetrahedral geometry with two phosphorus atoms from two triphenylphosphine ligands, thione sulfur of thiosemicarbazone ligand and chloride ion occupying the four corners of the tetrahedron. The structure of complex 3 was in contrast to sulfur-bridged dinuclear complex of copper(I) chloride with benzaldehydethiosemicarbazone, [Cu2Cl2(μ 2-S-Hbtsc)2(Ph3P)2] 2H2O. The intermolecular H-bonding, Cl ?HC ph, 2.733 ? and π interactions, {CHph?π, 2.796; 2.776 ?} in this complex led to the formation of 1D chain. Two such 1D chains were cross-linked via, Cl ?HC ph, 2.896 ? H-bonding to form a 2D network. [Figure not available: see fulltext.]
Aryl hydrazones linked thiazolyl coumarin hybrids as potential urease inhibitors
Hussain, Shafqat,Khan, Farman Ali,Khan, Khalid Mohammed,Lodhi, Muhammad Arif,Naz, Fouzia,Perveen, Shahnaz,Qureshi, Bakhtawer,Salar, Uzma,Taha, Muhammad,Ul?Haq, Zaheer
, (2021/08/20)
Aryl hydrazones bearing thiazolyl coumarin hybrids 1–32 were prepared by following 'one-pot' two-steps reaction scheme. Various arylaldehydes were reacted to thiosemicarbazide under acidic condition to form aryl thiosemicarbazone intermediates which in turn treated with 3-bromoacetyl coumarin under basic condition to afford thiazolyl coumarin hybrids 1–32. All hybrids were recognized by EI- and HREI-MS and 1H- and 13C-NMR spectroscopic techniques. Compounds 1–32 were screened for in vitro inhibitory activity against urease enzyme and displayed good to moderate inhibitory potential in the ranges of IC50 = 16.29 ± 1.1–256.30 ± 1.4?μM. Worth stating that compound 21 (IC50 = 16.29 ± 1.1?μM) was identified as more potent urease inhibitor than the standard acetohydroxamic acid (IC50 = 27.0 ± 0.5?μM). Derivatives 19 (IC50 = 77.67 ± 1.5?μM) and 30 (IC50 = 71.21 ± 1.6?μM) were found to be moderately active. Structure–activity relationship revealed that -F, -Cl, -OH, and -OMe groups and their respective positions on aryl ring are playing important role in urease enzyme inhibition. Molecular docking studies identified important interaction between the ligand (active hybrids) and urease active site.
Synthesis, characterization, alkaline phosphatase inhibition assay and molecular modeling studies of 1-benzylidene-2-(4-tert- butylthiazol-2-yl) hydrazines
Aziz, Hamid,Mahmood, Abid,Zaib, Sumera,Saeed, Aamer,El-Seedi, Hesham R.,Pelletier, Julie,Sévigny, Jean,Iqbal, Jamshed
, p. 6140 - 6153 (2020/08/14)
Alkaline phosphatases are homodimeric protein enzymes which removes phosphates from several types of molecules. These catalyze the hydrolysis of monoesters in phosphoric acid which in turn catalyze a transphosphorylation reaction. Thiazoles are a privileged class of heterocyclic compounds which may potentially serve as effective phosphatase inhibitors. In this regard, the present research paper reports the facile synthesis and characterization of substituted 1-benzylidene-2-(4-tert-butylthiazol-2-yl) hydrazines with excellent yields. The synthesized compounds were tested for inhibitory potential against alkaline phosphatases. The compound 1-(4-Hydroxy, 3-methoxybenzylidene)-2-(4-tert-butylthiazol-2-yl) hydrazine (5e) was found to be the most potent inhibitor of human tissue non-alkaline phosphatase in this group of molecules with an IC50 value of 1.09 ± 0.18 μM. The compound 1-(3,4-dimethoxybenzylidene)-2-(4-tert-butylthiazol-2-yl) hydrazine (5d) exhibited selectivity and potency for human intestinal alkaline phosphatase with an IC50 value of 0.71 ± 0.02 μM. In addition, structure activity relationship and molecular docking studies were performed to evaluate their binding modes with the target site of alkaline phosphatase. The docking analysis revealed that the most active inhibitors showed the important interactions within the binding pockets of human intestinal alkaline phosphatase and human tissue non-alkaline phosphatase and may be responsible for the inhibitory activity of the compound towards the enzymes. Therefore, the screened thiazole derivatives provided an outstanding platform for further development of alkaline phosphatase inhibitors.