37460-93-8Relevant academic research and scientific papers
Synthesis, molecular modeling study, preliminary antibacterial, and antitumor evaluation of N-substituted naphthalimides and their structural analogues
El-Azab, Adel S.,Alanazi, Amer M.,Abdel-Aziz, Naglaa I.,Al-Suwaidan, Ibrahim A.,El-Sayed, Magda A. A.,El-Sherbeny, Magda A.,Abdel-Aziz, Alaa A.-M.
, p. 2360 - 2375 (2013)
Carboxylic acid imides 1-26 have been synthesized and screened for their antibacterial against gram-positive and gram-negative organisms and their antitumor activity against 60 tumor cell lines taken from nine different organs. Compounds 12, 14, and 16 we
Molecular design, synthesis and biological evaluation of cyclic imides bearing benzenesulfonamide fragment as potential COX-2 inhibitors. Part 2
Al-Suwaidan, Ibrahim A.,Alanazi, Amer M.,El-Azab, Adel S.,Al-Obaid, Abdulrahman M.,Eltahir, Kamal E.H.,Maarouf, Azza R.,Abu El-Enin, Mohamed A.,Abdel-Aziz, Alaa A.-M.
, p. 2601 - 2605 (2013/06/27)
A group of cyclic imides (1-10) was designed for evaluation as a selective COX-2 inhibitors and investigated in vivo for their anti-inflammatory activity. Compounds 6a, 6b, 8a, 8b, 9a, 9b, 10a and 10b were proved to be potent COX-2 inhibitors with IC50 range of 0.1-4.0 μM. In vitro COX-1/COX-2 inhibition structure-activity studies identified compound 8a as a highly potent (IC50 = 0.1 μM), and an extremely selective [COX-2 (SI) > 1000] comparable to celecoxib [COX-2 (SI) > 384], COX-2 inhibitor that showed superior anti-inflammatory activity (ED50 = 72.4 mg/kg) relative to diclofenac (ED50 = 114 mg/kg). Molecular modeling was carried out through docking the designed compounds into the COX-2 binding site to predict if these compounds have analogous binding mode to the COX-2 inhibitors. The study showed that the homosulfonamide fragment of 8a inserted deep inside the 2 -pocket of the COX-2 active site, where the SO2NH2 group underwent H-bonding interaction with Gln192(2.95 A?), Phe 518(2.82 A?) and Arg513(2.63 and 2.73 A?). Docking study of the synthesized compound 8a into the active site of COX-2 revealed a similar binding mode to SC-558, a selective COX-2 inhibitor.
