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

Producció científica: Article en revista indexadaArticleAvaluat per experts

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Resum

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.

Idioma originalAnglès
Pàgines (de-a)5270-5273
Nombre de pàgines4
RevistaBioorganic and Medicinal Chemistry Letters
Volum19
Número17
DOIs
Estat de la publicacióPublicada - 1 de set. 2009

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