Interaction of Carthamus tinctorius lignan arctigenin with the binding site of tryptophan‐degrading enzyme indoleamine 2, 3‐dioxygenase. Issue 1 (7th September 2013)

• Record Type: Journal Article
• Authors: Temml, Veronika; Kuehnl, Susanne; Schuster, Daniela; Schwaiger, Stefan; Stuppner, Hermann; Fuchs, Dietmar
• Is Part Of: FEBS open bio. Volume 3:Issue 1(2013)
• Page Start: 450
• Page End: 452
• Publication Date: 2013-09-07
• Subjects: Lignan -- Carthamus tinctorius -- Indoleamine-2, 3-dioxygenase; Molecular biology -- Periodicals; Cytology -- Periodicals; Life sciences -- Periodicals; Biological Science Disciplines -- Periodicals; Molecular Biology -- Periodicals; Cell Biology -- Periodicals; Cytology; Life sciences; Molecular biology; Periodicals; 572.805
• DOI: 10.1016/j.fob.2013.08.008
• Languages: English
• ISSNs: 2211-5463

Abstract

Abstract : 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. Abstract : Mediterranean Carthamus tinctorius (Safflower) is used in traditional medicine. Indoleamine 2, 3‐dioxygenase (IDO) enzyme plays a role in inflammatory conditions and neuropsychiatric disorders. A potential direct influence of C. tinctorius lignans on IDO enzyme was examined. Computational calculations based on 3D geometry of the lignans were performed. Data suggest an intense interaction of lignan arctigenin with the IDO binding site.