460094-85-3Relevant articles and documents
De novo design, synthesis and evaluation of benzylpiperazine derivatives as highly selective binders of Mcl-1
Ding, Xiao,Li, Yan,Lv, Li,Zhou, Mi,Han, Li,Zhang, Zhengxi,Ba, Qian,Li, Jingquan,Wang, Hui,Liu, Hong,Wang, Renxiao
, p. 1986 - 2014 (2014/01/06)
Considerable efforts have been made to the development of small-molecule inhibitors of antiapoptotic B-cell lymphoma 2 (Bcl-2) family proteins (such as Bcl-2, Bcl-xL, and Mcl-1) as a new class of anticancer therapies. Unlike general inhibitors
Synthesis and structure-activity relationships of 4-hydroxy-4-phenylpiperidines as nociceptin receptor ligands: Part 2
Ho, Ginny D.,Bercovici, Ana,Tulshian, Deen,Greenlee, William J.,Fawzi, Ahmad,Fernandez, Xiomara,McLeod, Robbie L.,Smith Torhan, April,Zhang, Hongtao
, p. 3028 - 3033 (2008/02/02)
A series of 4-[2-(aminomethyl)phenyl]-1-[bis(2-chlorophenyl)methyl]-4-hydroxypiperidine analogs has been identified as nociceptin receptor ligands. These compounds display high affinity and functional activity at the nociceptin receptor. The synthesis and
N-sulfonylcarboximidamide apoptosis promoters
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Page/Page column 21, (2008/06/13)
Compounds having the formula are apoptosis promoters. Also disclosed are methods of making the compounds, compositions containing the compounds, and methods of treatment using the compounds.
Design, synthesis and biological evaluation of ambenonium derivatives as AChE inhibitors
Bolognesi, Maria Laura,Cavalli, Andrea,Andrisano, Vincenza,Bartolini, Manuela,Banzi, Rita,Antonello, Alessandra,Rosini, Michela,Melchiorre, Carlo
, p. 917 - 928 (2007/10/03)
Ambenonium (1), an old AChE inhibitor, is endowed with an outstanding affinity and a peculiar mechanism of action that, taken together, make it a very promising pharmacological tool for the treatment of Alzheimer's disease (AD). Unfortunately, the bisquaternary structure of 1 prevents its passage through the blood brain barrier. In a search of centrally active ambenonium derivatives, we planned to synthesize tertiary amines of 1, such as 2 and 3. In addition, to add new insights into the binding mechanism of the inhibitor, we designed constrained analogues of ambenonium by incorporating the diamine functions into cyclic moieties (4-12). The biological evaluation of the new compounds has been assessed in vitro against human AChE and BChE. All tertiary amine derivatives resulted more than 1000-fold less potent than 1 and, unlike prototype, did not show any selectivity between the two enzymes. This result, because of recent findings concerning the role of BChE in AD, makes our compounds, endowed with a well-balanced profile of AChE/BChE inhibition, valuable candidates for further development. To better clarify the interactions that account for the high affinity of 1, docking simulations and molecular dynamics studies on the AChE-1 complex were also carried out.