121365-22-8Relevant articles and documents
One-Pot Synthesis of 2,5-Disubstituted Furans through In Situ Formation of Allenes and Enolization Cascade
Bernhard, Yann,Gilbert, Joachim,Bousquet, Till,Favrelle-Huret, Audrey,Zinck, Philippe,Pellegrini, Sylvain,Pelinski, Lydie
, p. 7870 - 7873 (2019/12/24)
A one-pot synthesis of 2,5-disubstituted furans from γ-ketoacids is reported. In situ formation of allenoates by action of chloroformate on carboxylic acid following by enolization of ketone affords furan derivatives by cyclization. The reaction was extended to a wide scope of ketoacids and phosphonium salts. This methodology was applied on levulinic acid and derivatives, one of the biosourced platform chemicals.
Synthesis and binding study of certain 6-arylalkanamides as molecular probes for cannabinoid receptor subtypes
Taher, Azza T.,Kadry, Hanan H.,Allar, Marco,Di Marzo, Vincenzo,Abadi, Ashraf H.,Abouzid, Khaled A.
, p. 436 - 439 (2015/02/19)
Tetrahydrocannabinol and other mixed cannabinoid (CB) receptors CB1/CB2 receptor agonists are well established to elicit antinociceptive effects and psychomimetic actions, however, their potential for abuse have dampened enthusiasm f
Analogs design, synthesis and biological evaluation of peptidomimetics with potential anti-HCV activity
Lasheen, Deena S.,Ismail, Mohamed A.H.,Abou El Ella, Dalal A.,Ismail, Nasser S.M.,Eid, Sameh,Vleck, Susan,Glenn, Jeffrey S.,Watts, Andrew G.,Abouzid, Khaled A.M.
, p. 2742 - 2755 (2013/06/27)
Two series of peptidomimetics were designed, prepared and evaluated for their anti-HCV activity. One series possesses a C-terminal carboxylate functionality. In the other series, the electrophilic vinyl sulfonate moiety was introduced as a novel class of HCV NS3/4A protease inhibitors. In vitro based studies were then performed to evaluate the efficacies of the inhibitors using Human hepatoma cells, with the vinyl sulfonate ester (10) in particular, found to have highly potent anti-HCV activity with an EC50 = 0.296 μM. Finally, molecular modeling studies were performed through docking of the synthesized compounds in the HCV NS3/4A protease active site to assess their binding modes with the enzyme and gain further insight into their structure-activity relationships.
