The binding of xanthone derivatives to transthyretin

• Tipo: Artigo em Revista Científica Internacional
• Data: 2005

Autores

Maia, F (Autor) Outra; Almeida, MD (Autor) ICBAS; Gales, L (Autor) ICBAS; Kijjoa, A (Autor) ICBAS; Pinto, MMM (Autor) FFUP; Saraiva, MJ (Autor) ICBAS; Damas, AM (Autor) ICBAS

Revista

Título: Biochemical Pharmacology

Vol. 70

Páginas: 1861-1869

ISSN: 0006-2952

Editora: Elsevier

Indexação

ISI Web of Knowledge - 30 Citações

Scopus - 32 Citações

Classificação Científica

FOS: Ciências médicas e da saúde > Medicina básica

Outras Informações

ID Authenticus: P-000-02W

DOI: 10.1016/j.bcp.2005.09.012

Abstract (EN): A series of xanthone derivatives, isolated from Calophyllum teysmannii var. inophylloide, have been evaluated for their binding affinity to transthyretin. Transthyrefin 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.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 9