title: The binding of xanthone derivatives to transthyretin.
abstract: A series of xanthone derivatives, isolated from Calophyllum teysmannii var. inophylloide, have been evaluated for their binding affinity to transthyretin. Transthyretin is a plasma protein involved in the transport of thyroxine (T4) and also implicated in amyloid diseases. Using competition-binding studies with the protein natural ligand T4, we have identified one prenylated xanthone with a very strong affinity to transthyretin. Molecular docking simulations show that the flexible tail of the prenylated xanthone could allow favorable molecular interactions. Since this xanthone may play a role in the thyroxine metabolism and/or over the pathogenic process associated with the amyloid disease, these results may be explored for the design of new ligands.
authors.affiliation: Unidade de Estrutura Molecular, IBMC-Instituto de Biologia Molecular e Celular, Universidade do Porto, 4150-180 Porto, Portugal.
authors.forename: Filipe
authors.initials: F
authors.lastname: Maia
authors.forename: Maria do Rosário
authors.initials: Mdo R
authors.lastname: Almeida
authors.forename: Luís
authors.initials: L
authors.lastname: Gales
authors.forename: Anake
authors.initials: A
authors.lastname: Kijjoa
authors.forename: Madalena M M
authors.initials: MM
authors.lastname: Pinto
authors.forename: Maria J
authors.initials: MJ
authors.lastname: Saraiva
authors.forename: Ana M
authors.initials: AM
authors.lastname: Damas
mesh_terms: D001667:Binding, Competitive; D003461:Crystallography; D006801:Humans; D011228:Prealbumin / Q000737:chemistry / Q000378:metabolism*; D013329:Structure-Activity Relationship; D044004:Xanthones / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology
chemical_list: D011228:Prealbumin; D044004:Xanthones