Autor: |
Seyedi SM; Department of Chemistry, Faculty of Sciences, Ferdowsi University of Mashhad, Mashhad, Islamic Republic of Iran. smseyedi@yahoo.com, Eshghi H, Jafari Z, Attaran N, Sadeghian H, Saberi MR, Riazi MM |
Jazyk: |
angličtina |
Zdroj: |
Bioorganic & medicinal chemistry [Bioorg Med Chem] 2009 Feb 15; Vol. 17 (4), pp. 1614-22. Date of Electronic Publication: 2009 Jan 06. |
DOI: |
10.1016/j.bmc.2008.12.065 |
Abstrakt: |
A group of 4-allyloxyaniline amides 5a-o were designed, synthesized and evaluated as potential inhibitors of soybean 15-lipoxygenase (SLO) on the basis of eugenol and esteragol structures. Compound 5e showed the best IC(50) in SLO inhibition (IC(50)=0.67+/-0.06 microM). All compounds were docked in SLO active site retrieved from RCSB Protein Data Bank (PDB entry: 1IK3) and showed that allyloxy group of compounds is oriented towards the Fe(3+)-OH moiety in the active site of enzyme and fixed by hydrogen bonding with two conserved His(513) and Gln(716). It is resulted that molecular volume of the amide moiety would be a major factor in inhibitory potency variation of the synthetic amides, where the hydrogen bonding of the amide group could also involve in the activity of the inhibitors. |
Databáze: |
MEDLINE |
Externí odkaz: |
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