Design and synthesis of 3-alkyl-2-aryl-1,3-thiazinan-4-one derivatives as selective cyclooxygenase (COX-2) inhibitors

Bioorganic and Medicinal Chemistry Letters

Volumn 19, Issue 12, 2009, Pages 3162-3165

  Zebardast, Tannaz ^a   Zarghi, Afshin ^a   Daraie, Bahram ^b   Hedayati, Mehdi ^a   Dadrass, Orkideh G ^c  

^a SHAHID BEHESHTI UNIVERSITY OF MEDICAL SCIENCES   (Iran)

^b TARBIAT MODARES UNIVERSITY   (Iran)

^c ISLAMIC AZAD UNIVERSITY   (Iran)

Author keywords

1,3 Thiazinan 4 ones; COX 2 inhibition, SAR

Indexed keywords

3 BENZYL 2 (4 METHYLSULFONYLPHENYL) 1,3 THIAZINAN 4 ONE; CYCLOOXYGENASE 1; CYCLOOXYGENASE 2; CYCLOOXYGENASE 2 INHIBITOR; THIAZINE DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; DRUG DESIGN; DRUG POTENCY; DRUG SYNTHESIS; ENZYME INHIBITION; ENZYME INHIBITOR COMPLEX; IC 50; IN VITRO STUDY; PHARMACOPHORE;

ANIMALS; ANTI-INFLAMMATORY AGENTS, NON-STEROIDAL; CYCLOOXYGENASE 2 INHIBITORS; DRUG DESIGN; INHIBITORY CONCENTRATION 50; MICE; STRUCTURE-ACTIVITY RELATIONSHIP; THIAZINES;

EID: 65749092068     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2009.04.125     Document Type: Article

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22. Docking studies were performed using Autodock software Version 3.0. The coordinates of the X-ray crystal structure of the selective COX-2 inhibitor SC-558 bound to the murine COX-2 enzyme was obtained from the RCSB Protein Data Bank (1cx2) and hydrogens were added. The ligand molecules were constructed using the Builder module and were energy minimized for 1000 iterations reaching a convergence of 0.01 kcal/mol Å. The energy minimized ligands were superimposed on SC-558 in the PDB file 1cx2 after which SC-558 was deleted. The purpose of docking is to search for favourable binding configuration between the small flexible ligands and the rigid protein. Protein residues with atoms greater than 7.5 Å from the docking box were removed for efficiency. Searching is conducted within a specified 3D docking box using annealing based on the Monte Carlo method and MMFF94 molecular mechanics force field for 8000 iterations. These docked structures were very similar to the minimized structures obtained initially. The quality of the docked structures was evaluated by measuring the intermolecular energy of the ligand-enzyme assembly.
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24. 2N\
25. 2S: C, 61.63; H, 7.56; N, 5.53. Found: C, 61.88; H, 7.77; N, 5.60. Satisfactory analysis for C, H, N was obtained for all the compounds within ±0.4% of the theoretical values.