20781-20-8Relevant articles and documents
Synthesis, NMR and X-ray characterisation of 6-substituted 4-amino-5-aryldiazenyl-1-arylpyridazinium salts
?im?nek, Petr,Pe?ková, Markéta,Bertolasi, Valerio,Machá?ek, Vladimír,Ly?ka, Antonín
, p. 8130 - 8137 (2005)
A new simple method has been used to prepare 6-substituted 4-(subst. amino)-5-aryldiazenyl-1-arylpyridazinium salts from N-methyl- or N-aryl-3-amino-1-phenylbut-2-en-1-ones and 4-aminopent-3-en-2-ones and substituted benzenediazonium tetrafluoroborates or hexafluorophosphates. The structure of selected derivatives was studied by means of 15N NMR spectra and X-ray.
Design and synthesis of neolamellarin a derivatives targeting heat shock protein 90
Jiang, Long,Yin, Ruijuan,Wang, Xueting,Dai, Jiajia,Li, Jing,Jiang, Tao,Yu, Rilei
, p. 24 - 33 (2017/04/21)
In this study, we designed and synthesized a novel family of neolamellarin A derivatives that showed high inhibitory activity toward heat shock protein 90 (Hsp90), a kinase associated with cell proliferation. The 3,4-bis(catechol)pyrrole scaffold and the benzyl group with methoxy modification at N position of pyrrole are essential to the Hsp90 inhibitory activity and cytotoxicity of these compounds. Western blot analysis demonstrated that these compounds induced dramatic depletion of the examined client proteins of Hsp90, and accelerated cancer cell apoptosis. Docking simulations suggested that the binding mode of 9p was similar to that of the VER49009, a potent inhibitor of Hsp90. Further molecular dynamics simulation indicated that the hydrophobic interactions as well as the hydrogen bonds contributed to the high affinity of 9p to Hsp90.
New efficient substrates for semicarbazide-sensitive amine oxidase/VAP-1 enzyme: Analysis by SARs and computational docking
Yraola, Francesc,García-Vicente, Silvia,Fernández-Recio, Juan,Albericio, Fernando,Zorzano, Antonio,Marti, Luc,Royo, Miriam
, p. 6197 - 6208 (2007/10/03)
Structure activity relationships for semicarbazide-sensitive amine oxidase/vascular adhesion protein-1 (SSAO/VAP-1) were studied using a library of arylalkylamine substrates, with the aim of contributing to the discovery of more efficient SSAO substrates. Experimental data were contrasted with computational docking studies, thereby allowing us to examine the mechanism and substrate-binding affinity of SSAO and thus contribute to the discovery of more efficient SSAO substrates and provide a structural basis for their interactions. We also built a model of the mouse SSAO structure, which provides several structural rationales for interspecies differences in SSAO substrate selectivity and reveals new trends in SSAO substrate recognition. In this context, we identified novel efficient substrates for human SSAO that can be used as a lead for the discovery of antidiabetic agents.