ChemInform Abstract: SPECIFIC OXIDATION OF β-HYDROXYSELENIDES TO α,β-UNSATURATED KETONES AND α-SELENO CARBONYL DERIVATIVES

1979 ◽  
Vol 10 (49) ◽  
Author(s):  
J. LUCCHETTI ◽  
A. KRIEF
Keyword(s):  
Unsaturated Ketones ◽  
Carbonyl Derivatives ◽  
Specific Oxidation

Mass Spectrometry in Structural and Stereochemical Problems. CCXVII. Electron Impact Promoted Fragmentation of O-Methyl Oximes of some α,β-Unsaturated Ketones and Methyl Substituted Cyclohexanones

1972 ◽  
Vol 50 (17) ◽  
pp. 2776-2785 ◽  
Author(s):  
Younus M. Sheikh ◽  
Raymond J. Liedtke ◽  
A. M. Duffield ◽  
Carl Djerassi
Keyword(s):  
Mass Spectrometry ◽  
Electron Impact ◽  
High Resolution Mass Spectrometry ◽  
Unsaturated Ketone ◽  
Deuterium Labeling ◽  
Oxime Ether ◽  
Ether Group ◽  
Unsaturated Ketones ◽  
Carbonyl Derivatives ◽  
Mass Spectrometric Fragmentation

Deuterium labeling and high resolution mass spectrometry have been utilized to delineate the modes of mass spectrometric fragmentation of O-methyl oximes of α,β-unsaturated ketones and methyl substituted cyclohexanones. α,β-Unsaturated ketone and 2- and 4-methylcyclohexanone O-methyl oxime ether derivatives fragment upon electron impact in a manner reminiscent of the carbonyl derivatives from which they were prepared. However, several fragmentation sequences characteristic of the O-methyl oxime ether group were observed.

1,4-Reductions of α,β-Unsaturated Ketones and Aldehydes via in situ Generated Hydridocuprates

Synlett ◽  
1989 ◽  
Vol 1989 (01) ◽  
pp. 64-66 ◽  
Author(s):  
Bruce H. Lipshutz ◽  
Christopher S. Ung ◽  
Saumitra Sengupta
Keyword(s):  
Unsaturated Ketones

Drug Design of Inhibitors of Alzheimer’s Disease (AD): POM and DFT Analyses of Cholinesterase Inhibitory Activity of β-amino di-Carbonyl Derivatives

2019 ◽  
Vol 19 (8) ◽  
pp. 688-705
Author(s):  
Taibi Ben Hadda ◽  
Abdur Rauf ◽  
Hsaine Zgou ◽  
Fatma Sezer Senol ◽  
Ilkay Erdogan Orhan ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Cholinesterase Inhibitors ◽  
Metal Accumulation ◽  
Microtiter Plate ◽  
Metal Chelation ◽  
Carbonyl Derivatives ◽  
Cholinesterase Inhibitory Activity ◽  
Inhibitory Potential

Background:Since deficit of acetylcholine has been evidenced in the Alzheimer’s disease (AD) patients, cholinesterase inhibitors are currently the most specified drug category for the remediation of AD.Method:In the present study, 16 compounds (1-16) with dicarbonyl skeletons have been synthesized and tested for their inhibitory potential in vitro against AChE and BChE using ELISA microtiter plate assays at 100 μg/mL. Since metal accumulation is related to AD, the compounds were also tested for their metal-chelation capacity.Results and Conclusion:All the investigated dicarbonyl compounds exerted none or lower than 30% inhibition against both cholinesterases, whereas compounds 2, 8 and 11 showed 37, 42, 41% of inhibition towards BChE, being the most active. The highest metal-chelation capacity was observed with compound 8 (53.58 ± 2.06%). POM and DFT analyses are in good harmonization with experimental data.

Design, Synthesis and Biological Evaluation: 5-amino-1H-pyrazole-1- carbonyl derivatives as FGFR Inhibitors

2020 ◽  
Vol 17 (11) ◽  
pp. 1330-1341
Author(s):  
Yan Zhang ◽  
Niefang Yu
Keyword(s):  
Cancer Cells ◽  
Cell Lines ◽  
Cancer Cell ◽  
Cancer Cell Lines ◽  
Biological Evaluation ◽  
Human Gastric Cancer ◽  
Design Synthesis ◽  
Carbonyl Derivatives ◽  
Ic50 Values ◽  
Inhibitory Activities

Background: Fibroblast growth factors (FGFs) and their high affinity receptors (FGFRs) play a major role in cell proliferation, differentiation, migration, and apoptosis. Aberrant FGFR signaling pathway might accelerate development in a broad panel of malignant solid tumors. However, the full application of most existing small molecule FGFR inhibitors has become a challenge due to the potential target mutation. Hence, it has attracted a great deal of attention from both academic and industrial fields for hunting for novel FGFR inhibitors with potent inhibitory activities and high selectivity. Objective: Novel 5-amino-1H-pyrazole-1-carbonyl derivatives were designed, synthesized, and evaluated as FGFR inhibitors. Methods: A series of 5-amino-1H-pyrazole-1-carbonyl derivatives were established by a condensation of the suitable formyl acetonitrile derivatives with either hydrazine or hydrazide derivatives in the presence of anhydrous ethanol or toluene. The inhibitory activities of the target compounds were screened against the FGFRs and two representative cancer cell lines. Tests were carried out to observe the inhibition of 8e against FGFR phosphorylation and downstream signal phosphorylation in human gastric cancer cell lines (SNU-16). The molecular docking of all the compounds were performed using Molecular Operating Environment in order to evaluate their binding abilities with the corresponding protein kinase. Results: A series of 5-amino-1H-pyrazole-1-carbonyl derivatives have been designed and synthesized, screened for their inhibitory activities against FGFRs and cancer cell lines. Most of the target compounds showed moderate to good anti-proliferate activities against the tested enzymes and cell lines. The most promising compounds 8e suppressed FGFR1-3 with IC50 values of 56.4, 35.2, 95.5 nM, and potently inhibited the SNU-16 and MCF-7 cancer cells with IC50 values of 0.71 1.26 μM, respectively. And 8e inhibited the growth of cancer cells containing FGFR activated by multiple mechanisms. In addition, the binding interactions were quite similar in the molecular models between generated compounds and Debio-1347 with the FGFR1. Conclusion: According to the experimental findings, 5-amino-1H-pyrazole-1-carbonyl might serve as a promising template of an FGFR inhibitor.

The Binding and Viscometric Studies of Ni+2, Co+2 and Mn+2 Ions with Protein by Spectrometric and pH Metric Techniques

2019 ◽  
Vol 9 (2) ◽  
pp. 151-162
Author(s):  
Shveta Acharya ◽  
Arun Kumar Sharma
Keyword(s):  
Metal Ions ◽  
Metal Ion ◽  
Protein Molecule ◽  
Vital Role ◽  
Sufficient Evidence ◽  
Structural Requirement ◽  
Nickel Ions ◽  
Cobalt Ions ◽  
Lower Temperature ◽  
Specific Oxidation

Background: The metal ions play a vital role in a large number of widely differing biological processes. Some of these processes are quite specific in their metal ion requirements. In that only certain metal ions, in specific oxidation states, can full fill the necessary catalytic or structural requirement, while other processes are much less specific. Objective: In this paper we report the binding of Mn (II), Ni (II) and Co (II) with albumin are reported employing spectrophotometric and pH metric method. In order to distinguish between ionic and colloidal linking, the binding of metal by using pH metric and viscometric methods and the result are discussed in terms of electrovalent and coordinate bonding. Methods: The binding of Ni+2, Co+2 and Mn+2 ions have been studied with egg protein at different pH values and temperatures by the spectrometric technique. Results: The binding data were found to be pH and temperature dependent. The intrinsic association constants (k) and the number of binding sites (n) were calculated from Scatchard plots and found to be at the maximum at lower pH and at lower temperatures. Therefore, a lower temperature and lower pH offered more sites in the protein molecule for interaction with these metal ions. Statistical effects seem to be more significant at lower Ni+2, Co+2 and Mn+2 ions concentrations, while at higher concentrations electrostatic effects and heterogeneity of sites are more significant. Conclusion: The pH metric as well as viscometric data provided sufficient evidence about the linking of cobalt, nickel and manganese ions with the nitrogen groups of albumin. From the nature and height of curves in the three cases it may be concluded that nickel ions bound strongly while the cobalt ions bound weakly.

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