Hauptseite > Publikationsdatenbank > Discovery and structure activity relationship of small molecule inhibitors of toxic-ß--amyloid-42 fibril formation > print

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|a 10.1074/jbc.M112.357665
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|a Kroth, H.
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245 _ _ |a Discovery and structure activity relationship of small molecule inhibitors of toxic-ß--amyloid-42 fibril formation
260 _ _ |a Bethesda, Md.
|b Soc.
|c 2012
300 _ _ |a 34786 - 34800
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440 _ 0 |0 3091
|a Journal of Biological Chemistry
|v 287
|x 0021-9258
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Increasing evidence implicates Aβ peptides self-assembly and fibril formation as crucial events in the pathogenesis of Alzheimer disease. Thus, inhibiting Aβ aggregation, among others, has emerged as a potential therapeutic intervention for this disorder. Herein, we employed 3-aminopyrazole as a key fragment in our design of non-dye compounds capable of interacting with Aβ42 via a donor-acceptor-donor hydrogen bond pattern complementary to that of the β-sheet conformation of Aβ42. The initial design of the compounds was based on connecting two 3-aminopyrazole moieties via a linker to identify suitable scaffold molecules. Additional aryl substitutions on the two 3-aminopyrazole moieties were also explored to enhance π-π stacking/hydrophobic interactions with amino acids of Aβ42. The efficacy of these compounds on inhibiting Aβ fibril formation and toxicity in vitro was assessed using a combination of biophysical techniques and viability assays. Using structure activity relationship data from the in vitro assays, we identified compounds capable of preventing pathological self-assembly of Aβ42 leading to decreased cell toxicity.
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