Isatin derivatives, a novel class of transthyretin fibrillogenesis inhibitors

• Type: Article in International Scientific Journal
• Date: 2009

Authors

Asensio Gonzalez (Author) Other; Josefina Quirante (Author) Other; Joan Nieto (Author) Other; Maria Rosario Almeida (Author) ICBAS; Maria Joao Saraiva (Author) ICBAS; Antoni Planas (Author) Other; Gemma Arsequell (Author) Other; Gregorio Valencia (Author) Other

Journal

Title: Bioorganic and Medicinal Chemistry Letters

Vol. 19

Pages: 5270-5273

ISSN: 0960-894X

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 36 Citations

Scopus - 44 Citations

Scientific classification

FOS: Natural sciences > Chemical sciences

Other information

Authenticus ID: P-003-FYA

DOI: 10.1016/j.bmcl.2009.03.004

Abstract (EN): The isatin core structure was found to be a novel chemical scaffold in transthyretin (TTR) brillogenesis inhibitor design. Among the series of isatin analogues prepared and tested, the nitro compound 1,3-dihydro3-[(4-nitrophenyl)imino]-2H-indol-2-one (2r) is as potent as triiodophenol, which is one of the most active known TTR inhibitors. The E/Z stereochemistry of these molecules in solution, elucidated by (1)H NMR, does not influence their biological activity. The compounds do not bind to the native tetrameric TTR suggesting that their inhibitory action is independent of the protein binding and stabilization. (C) 2009 Published by Elsevier Ltd.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 4