15875-53-3Relevant academic research and scientific papers
Clean synthesis of 2-arylideneindan-1,3-diones in water
Yang, Peng Hui,Zhang, Qun Zheng,Sun, Wei
, p. 1063 - 1068 (2012)
A high-yield synthesis of 2-arylideneindan-1,3-diones in water was achieved by the Knoevenagel condensation of indan-1,3-dione with aromatic aldehydes at ambient temperature avoiding the addition of any catalyst. The procedure is simple, efficient, as wel
Indane-1,3-diones: As potential and selective α-glucosidase inhibitors, their synthesis, in vitro and in silico studies
Hameed, Shehryar,Iqbal, Jamshed,Kanwal,Khan, Khalid Mohammed,Khan, Shahid Ullah,Mukhtar, Asma,Perveen, Shahnaz,Shah, Shazia,Zaib, Sumera
, p. 887 - 902 (2021/10/21)
Background: Diabetes mellitus is one of the most chronic metabolic disorders. Since past few years, our research group had synthesized and evaluated libraries of heterocyclic compounds against α and β-glucosidase enzymes and found encouraging results. The current study comprises of evaluation of indane-1,3-dione as antidiabetic agents based on our previously reported results obtained from closely related moiety isatin and its derivatives. Objective: A library of twenty three indane-1,3-dione derivatives (1-23) was synthesized and evaluated for α and β-glucosidase inhibitions. Moreover, in silico docking studies were carried out to in-vestigate the putative binding mode of selected compounds with the target enzyme. Methods: The indane-1,3-dione derivatives (1-23) were synthesized by Knoevenagel condensation of different substituted benzaldehydes with indane-1,3-dione under basic condition. The structures of synthetic molecules were deduced by using different spectroscopic techniques, including1 H-,13 C-NMR, EI-MS, and CHN analysis. Compounds (1-23) were evaluated for α and β-glucosidase inhibitions by adopting the literature protocols. Result: Off twenty three, eleven compounds displayed good to moderate activity against α-glucosidase enzyme, nonetheless, all compounds exhibited less than 50% inhibition against β-glucosidase enzyme. Compounds 1, 14, and 23 displayed good activity against α-glucosidase enzyme with IC50 values of 2.80 ± 0.11, 0.76 ± 0.01, and 2.17 ± 0.18 μM, respectively. The results have shown that these compounds have selectively inhibited the α-glucosidase enzyme. The in silico docking studies also supported the above results and showed different types of interactions of synthetic molecules with the active site of enzyme. Conclusion: The compounds 1, 14, and 23 have shown good inhibition against α-glucosidase and may potentially serve as lead for the development of new therapeutic representatives.
Synthesis and characterization of 2-benzylidene-1,3-indandione derivatives as in vitro quantification of amyloid fibrils
Adibi, Hadi,Mehrabi, Maryam,Amiri, Kazhal,Balalaie, Saeed,Khodarahmi, Reza
, p. 423 - 432 (2019/11/03)
Timely detection of amyloid aggregations has a critical role in the treatment of degenerative nervous system disorders such as Alzheimer’s, Parkinson’s disease and systemic amyloidosis. Thioflavin T (ThT) is a dye considered for the detection of amyloids.
CLPX INHIBITORY COMPOUNDS FOR THE TREATMENT OF MULTI RESISTANT STAPHYLOCOCCUS AUREUS VIRULENCE AND FOR THE TREATMENT OF LEUKEMIA
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Page/Page column 32, (2018/07/26)
The present invention relates to antibiotic compounds and their use as ClpX inhibitors and in the treatment of bacterial infections, such as infections with multi-resistant Staphylococcus aureas, and in the treatment of leukemia. The present invention fur
A Chemical Disruptor of the ClpX Chaperone Complex Attenuates the Virulence of Multidrug-Resistant Staphylococcus aureus
Fetzer, Christian,Korotkov, Vadim S.,Th?nert, Robert,Lee, Kyu Myung,Neuenschwander, Martin,von Kries, Jens Peter,Medina, Eva,Sieber, Stephan A.
supporting information, p. 15746 - 15750 (2017/10/20)
The Staphylococcus aureus ClpXP protease is an important regulator of cell homeostasis and virulence. We utilized a high-throughput screen against the ClpXP complex and identified a specific inhibitor of the ClpX chaperone that disrupts its oligomeric sta
