1099643-39-6Relevant articles and documents
CITU: A Peptide and Decarboxylative Coupling Reagent
Degruyter, Justine N.,Malins, Lara R.,Wimmer, Laurin,Clay, Khalyd J.,Lopez-Ogalla, Javier,Qin, Tian,Cornella, Josep,Liu, Zhiqing,Che, Guanda,Bao, Denghui,Stevens, Jason M.,Qiao, Jennifer X.,Allen, Martin P.,Poss, Michael A.,Baran, Phil S.
, p. 6196 - 6199 (2017)
Tetrachloro-N-hydroxyphthalimide tetramethyluronium hexafluorophosphate (CITU) is disclosed as a convenient and economical reagent for both acylation and decarboxylative cross-coupling chemistries. Within the former set of reactions, CITU displays reactiv
New sulphonamide pyrolidine carboxamide derivatives: Synthesis, molecular docking, antiplasmodial and antioxidant activities
Onoabedje, Efeturi A.,Ibezim, Akachukwu,Okoro, Uchechukwu C.,Batra, Sanjay
, (2021/03/16)
Carboxamides bearing sulphonamide functionality have been shown to exhibit significant lethal effect on Plasmodium falciparum, the causative agent of human malaria. Here we report the synthesis of thirty-two new drug-like sulphonamide pyrolidine carboxami
Structure-based discovery of highly selective phosphodiesterase-9A inhibitors and implications for inhibitor design
Meng, Fei,Huang, Manna,Zhu, Xinhai,Wan, Yiqian,Hou, Jing,Shao, Yong-Xian,Cai, Yonghong,Li, Zhe,Xu, Jie,Liu, Peiqing,Luo, Hai-Bin,Ke, Hengming,Wu, Pei-Ying
, p. 8549 - 8558,10 (2020/09/15)
A new series of phosphodiesterase-9 (PDE9) inhibitors that contain a scaffold of 6-amino-pyrazolopyrimidinone have been discovered by a combination of structure-based design and computational docking. This procedure significantly saved the load of chemical synthesis and is an effective method for the discovery of inhibitors. The best compound 28 has an IC50 of 21 nM and 3.3 μM, respectively, for PDE9 and PDE5 and about 3 orders of magnitude of selectivity against other PDE families. The crystal structure of the PDE9 catalytic domain in complex with 28 has been determined and shows a hydrogen bond between 28 and Tyr424. This hydrogen bond may account for the 860-fold selectivity of 28 against PDE1B, in comparison with about 30-fold selectivity of BAY73-6691. Thus, our studies suggest that Tyr424, a unique residue of PDE8 and PDE9, is a potential target for improvement of selectivity of PDE9 inhibitors.
