600168-40-9Relevant articles and documents
Assembly of organosilver coordination frameworks with polycyclic benzenoid aromatic ethynide ligands
Hau, Sam C.K.,Mak, Thomas C.W.
, p. 123 - 133 (2015/08/18)
Abstract In a series of nine silver(I) complexes synthesized with ethynyl-functionalized condensed-ring benzenoid aromatics, the terminal ethynide group is invariably inserted into an argentophilic Agn (n = 4-5) basket, leading to the generation of coordination chains or multinuclear metallocycles via silver-aromatic interaction and strong face-to-face aromatic π-π stacking interaction. The coordination preferences of the ethynide ligand with respect to the size of the aromatic nucleus proved to be dominant factors in directing the construction of multi-dimensional organosilver(I) networks, which are consolidated by weak intermolecular interactions in supramolecular assembly.
Structure-guided design of A3 adenosine receptor-selective nucleosides: Combination of 2-arylethynyl and bicyclo[3.1.0]hexane substitutions
Tosh, Dilip K.,Deflorian, Francesca,Phan, Khai,Gao, Zhan-Guo,Wan, Tina C.,Gizewski, Elizabeth,Auchampach, John A.,Jacobson, Kenneth A.
supporting information; experimental part, p. 4847 - 4860 (2012/07/27)
(N)-Methanocarba adenosine 5′-methyluronamides containing known A3 AR (adenosine receptor)-enhancing modifications, i.e., 2-(arylethynyl)adenine and N6-methyl or N6-(3-substituted- benzyl), were nanomolar full agonists of human (h) A3AR and highly selective (Ki ～0.6 nM, N6-methyl 2-(halophenylethynyl) analogues 13 and 14). Combined 2-arylethynyl-N6-3-chlorobenzyl substitutions preserved A3AR affinity/selectivity in the (N)-methanocarba series (e.g., 3,4-difluoro full agonist MRS5698 31, K i 3 nM, human and mouse A3) better than that for ribosides. Polyaromatic 2-ethynyl N6-3-chlorobenzyl analogues, such as potent linearly extended 2-p-biphenylethynyl MRS5679 34 (Ki hA3 3.1 nM; A1, A2A, inactive) and fluorescent 1-pyrene adduct MRS5704 35 (Ki hA3 68.3 nM), were conformationally rigid; receptor docking identified a large, mainly hydrophobic binding region. The vicinity of receptor-bound C2 groups was probed by homology modeling based on recent X-ray structure of an agonist-bound A2AAR, with a predicted helical rearrangement requiring an agonist-specific outward displacement of TM2 resembling opsin. Thus, the X-ray structure of related A2AAR is useful in guiding the design of new A3AR agonists.
