1143-62-0Relevant articles and documents
Synthesis, Characterization, Molecular Docking, and Biological Activities of Some Natural and Synthetic Urolithin Analogs
Noshadi, Bahareh,Ercetin, Tugba,Luise, Chiara,Yuksel, Mine Yarim,Sippl, Wolfgang,Sahin, Mustafa Fethi,Gazi, Mustafa,Gulcan, Hayrettin Ozan
, (2020)
Urolithins (that is, hydroxy substituted benzo[c]chromen-6-one derivatives) are formed within the gastrointestinal tract following to the exposure to various ellagitannin rich diet, particularly involving pomegranate, nuts, and berries. Regarding the bioavailability deficiency of ellagitannins, the biological activities obtained through the extracts of these dietaries are attributed to the urolithin compounds, since they are bioavailable. Particularly, there are studies indicating the importance of ellagitannin-rich food for protective and alternative treatment of Alzheimer's Disease (AD). From this perspective, within this study, the major urolithins (that is, urolithins A and B), their methyl ether metabolites, as well as some synthetic urolithin analogs have been synthesized and screened for their biological activities in various enzyme inhibition (acetylcholinesterase, butyrylcholinesterase, monoamine oxidase B, cyclooxygenase 1, and cyclooxygenase 2) and antioxidant (DPPH radical scavenging) assay systems. The results pointed out the potential of urolithins to act as inhibitors on these receptors. Docking studies were also performed to investigate the possible interactions.
Oxidant-Free C(sp2)-H Functionalization/C-O Bond Formation: A Kolbe Oxidative Cyclization Process
Zhang, Lei,Zhang, Zhenxing,Hong, Junting,Yu, Jian,Zhang, Jianning,Mo, Fanyang
, p. 3200 - 3207 (2018)
An anodic oxidation/cyclization of 2-arylbenzoic acids for the synthesis of dibenzopyranones has been developed. The reaction proceeds at room temperature with no oxidant or electrolyte required and exhibits a high atom economy with H2 being th
Copper catalyzed room temperature lactonization of aromatic C-H bond: A novel and efficient approach for the synthesis of dibenzopyranones
Singha, Raju,Dhara, Shubhendu,Ghosh, Munmun,Ray, Jayanta K.
, p. 8801 - 8805 (2015)
We have developed a novel and efficient methodology for the intramolecular aryl C-H oxidative lactonization of 2-arylbenzaldehyde using a low-cost CuCl catalyst and TBHP as the oxidant at room temperature. We applied the methodology to the synthesis of a series of dibenzopyranones.
Urolithin and reduced urolithin derivatives as potent inhibitors of tyrosinase and melanogenesis: Importance of the 4-substituted resorcinol moiety
Lee, Sanggwon,Choi, Heejeong,Park, Yujin,Jung, Hee Jin,Ullah, Sultan,Choi, Inkyu,Kang, Dongwan,Park, Chaeun,Ryu, Il Young,Jeong, Yeongmu,Hwang, Yeji,Hong, Sojeong,Chun, Pusoon,Moon, Hyung Ryong
, (2021)
We previously reported (E)-β-phenyl-α,β-unsaturated carbonyl scaffold ((E)-PUSC) played an important role in showing high tyrosinase inhibitory activity and that derivatives with a 4-substituted resorcinol moiety as the β-phenyl group of the scaffold resulted in the greatest tyrosi-nase inhibitory activity. To examine whether the 4-substituted resorcinol moiety could impart tyro-sinase inhibitory activity in the absence of the α,β-unsaturated carbonyl moiety of the (E)-PUSC scaffold, 10 urolithin derivatives were synthesized. To obtain more candidate samples, the lactone ring in synthesized urolithins was reduced to produce nine reduced urolithins. Compounds 1c (IC50 = 18.09 ± 0.25 μM), 1h (IC50 = 4.14 ± 0.10 μM), and 2a (IC50 = 15.69 ± 0.40 μM) had greater mushroom tyrosinase-inhibitory activities than kojic acid (KA) (IC50 = 48.62 ± 3.38 μM). The SAR results suggest that the 4-substituted resorcinol motif makes an important contribution to tyrosinase inhibition. To investigate whether these compounds bind to human tyrosinase, a human tyrosinase homology model was developed. Docking simulations with mushroom and human tyrosinases showed that 1c, 1h, and 2a bind to the active site of both tyrosinases with higher binding affinities than KA. Pharmacophore analyses showed that two hydroxyl groups of the 4-substituted resorcinol entity act as hydrogen bond donors in both mushroom and human tyrosinases. Kinetic analyses indicated that these compounds were all competitive inhibitors. Compound 2a inhibited cellular tyrosinase activity and melanogenesis in α-MSH plus IBMX-stimulated B16F10 melanoma cells more strongly than KA. These results suggest that 2a is a promising candidate for the treatment of skin pigment disorders, and show the 4-substituted resorcinol entity importantly contributes to tyrosinase inhi-bition.
Design, synthesis, and biological evaluation of novel 6h-benzo[c]chromen-6-one derivatives as potential phosphodiesterase ii inhibitors
Tang, Long,Jiang, Jianchun,Song, Guoqiang,Wang, Yajing,Zhuang, Ziheng,Tan, Ying,Xia, Yan,Huang, Xianfeng,Feng, Xiaoqing
, (2021/05/29)
Urolithins (hydroxylated 6H-benzo[c]chromen-6-ones) are the main bioavailable metabolites of ellagic acid (EA), which was shown to be a cognitive enhancer in the treatment of neurodegenerative diseases. As part of this research, a series of alkoxylated 6H-benzo[c]chromen-6-one derivatives were designed and synthesized. Furthermore, their biological activities were evaluated as potential PDE2 inhibitors, and the alkoxylated 6H-benzo[c]chromen-6-one derivative 1f was found to have the optimal inhibitory potential (IC50: 3.67 ± 0.47 μM). It also exhibited comparable activity in comparison to that of BAY 60-7550 in vitro cell level studies.
Cerium photocatalyzed dehydrogenative lactonization of 2-arylbenzoic acids
Wadekar, Ketan,Aswale, Suraj,Yatham, Veera Reddy
supporting information, p. 983 - 987 (2020/02/15)
The first cerium photocatalyzed dehydrogenative lactonization of 2-arylbenzoic acids has been developed. This operationally simple protocol allows rapid access to synthetically useful coumarins on gram scale by employing CeCl3 as a photocatalyst and O2 as a terminal oxidant. Overall, this delivers an economical and environmentally amiable entry to diversely substituted coumarins, important structural motifs in bioactive molecules.