The binding of xanthone derivatives to transthyretin

• Type: Article in International Scientific Journal
• Date: 2005

Authors

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

Journal

Title: Biochemical Pharmacology

Vol. 70

Pages: 1861-1869

ISSN: 0006-2952

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 30 Citations

Scopus - 32 Citations

Scientific classification

FOS: Medical and Health sciences > Basic medicine

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 9