Open AccessInteraction of Carthamus tinctorius lignan arctigenin with the binding site of tryptophan‐degrading enzyme indoleamine 2,3‐dioxygenase
Author(s) -
Temml Veronika,
Kuehnl Susanne,
Schuster Daniela,
Schwaiger Stefan,
Stuppner Hermann,
Fuchs Dietmar
Publication year - 2013
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1016/j.fob.2013.08.008
Subject(s) - carthamus , indoleamine 2,3 dioxygenase , docking (animal) , enzyme , dioxygenase , tryptophan , chemistry , biochemistry , stereochemistry , lignan , binding site , enzyme assay , biology , traditional medicine , medicine , nursing , amino acid
Mediterranean Carthamus tinctorius (Safflower) is used for treatment of inflammatory conditions and neuropsychiatric disorders. Recently C. tinctorius lignans arctigenin and trachelogenin but not matairesinol were described to interfere with the activity of tryptophan‐degrading enzyme indoleamine 2,3‐dioxygenase (IDO) in peripheral blood mononuclear cells in vitro . We examined a potential direct influence of compounds on IDO enzyme activity applying computational calculations based on 3D geometry of the compounds. The interaction pattern analysis and force field‐based minimization was performed within LigandScout 3.03, the docking simulation with MOE 2011.10 using the X‐ray crystal structure of IDO. Results confirm the possibility of an intense interaction of arctigenin and trachelogenin with the binding site of the enzyme, while matairesinol had no such effect.