332104-52-6Relevant academic research and scientific papers
Design, synthesis, and biological and crystallographic evaluation of novel inhibitors of plasmodium falciparum enoyl-ACP-reductase (pf fabi)
Belluti, Federica,Perozzo, Remo,Lauciello, Leonardo,Colizzi, Francesco,Kostrewa, Dirk,Bisi, Alessandra,Gobbi, Silvia,Rampa, Angela,Bolognesi, Maria Laura,Recanatini, Maurizio,Brun, Reto,Scapozza, Leonardo,Cavalli, Andrea
, p. 7516 - 7526 (2013)
Malaria, a disease of worldwide significance, is responsible for over one million deaths annually. The liver-stage of Plasmodium's life cycle is the first, obligatory, but clinically silent step in malaria infection. The P. falciparum type II fatty acid biosynthesis pathway (PfFAS-II) has been found to be essential for complete liver-stage development and has been regarded as a potential antimalarial target for the development of drugs for malaria prophylaxis and liver-stage eradication. In this paper, new coumarin-based triclosan analogues are reported and their biological profile is explored in terms of inhibitory potency against enzymes of the PfFAS-II pathway. Among the tested compounds, 7 and 8 showed the highest inhibitory potency against Pf enoyl-ACP-reductase (PfFabI), followed by 15 and 3. Finally, we determined the crystal structures of compounds 7 and 11 in complex with PfFabI to identify their mode of binding and to confirm outcomes of docking simulations.
Synthesis of 2-phenylbenzofuran derivatives and selective binding activities on estrogen receptor
Zhang, Ping,Yang, Yewei,Zheng, Xiaoliang,Huang, Wenhai,Ma, Zhen,Shen, Zhengrong
scheme or table, p. 270 - 274 (2012/03/11)
An improved chemical reaction protocol with short time and easy work-up was described here for 2-phenylbenzofuran derivatives. The final purified products, 2-phenylbenzofuran derivatives 5a-g and the intermediate diols 4a-g, were evaluated for their estrogen receptor (ER) binding affinity and selective activity in vitro. Among these fourteen tested compounds, 4g and 5g showed higher binding affinity on ER subtypes, ERα and ERβ. Compound 4g exhibited preferable ERα binding, while 5g was more estrogen selective for ERβ. The molecular docking was also performed to explore the detailed interactive interface between ER and the compounds.
