structural stabilization of transthyretin by a new compound, 6-benzoyl-2-hydroxy-1h-benzo[de]isoquinoline-1,3(2h)-dione
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2015
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Abstract
Familial amyloid polyneuropathy (FAP) is a genetic, adult-onset, neurodegenerative disorder caused by amyloid formation of transthyretin (TTR), a thyroxine-binding protein. Mutation in TTR causes a propensity of TTR tetramer to dissociate to monomer, which is the first step to amyloidosis. Thus, a drug that can stabilize the tetramer structure will have therapeutic benefit. Here, by virtual screening and biochemical assays, we identified small molecule 6-benzoyl-2-hydroxy-1H-benzo[de]isoquinoline-1,3(2H)-dione (L6) that can prevent the dissociation of TTR to monomer. X-ray crystallography reveals that L6 binds to the T4 binding pocket of TTR. These findings show that L6 is a candidate TTR stabilizer.
| Reference Key |
yokoyama2015journalstructural
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|---|---|
| Authors | ;Takeshi Yokoyama;Shun Takaki;Keisuke Chosa;Takashi Sato;Mary Ann Suico;Yuriko Teranishi;Tsuyoshi Shuto;Mineyuki Mizuguchi;Hirofumi Kai |
| Journal | plant direct |
| Year | 2015 |
| DOI |
10.1016/j.jphs.2015.09.006
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| URL | |
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