Isatin derivatives, a novel class of transthyretin fibrillogenesis inhibitors

Asensio González, Josefina Quirante, Joan Nieto, Maria Rosário Almeida, Maria Joao Saraiva, Antoni Planas, Gemma Arsequell, Gregorio Valencia

Research output: Indexed journal article Articlepeer-review

47 Citations (Scopus)


The isatin core structure was found to be a novel chemical scaffold in transthyretin (TTR) fibrillogenesis inhibitor design. Among the series of isatin analogues prepared and tested, the nitro compound 1,3-dihydro-3-[(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 1H 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.

Original languageEnglish
Pages (from-to)5270-5273
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Issue number17
Publication statusPublished - 1 Sept 2009


  • Amyloidosis
  • Inhibitors
  • Isatins
  • Transthyretin


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