Molecular modeling of anti-amyloidal catechol derivatives using amyloidogenic proteins

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Molecular modeling of anti-amyloidal catechol derivatives was performed using Amyloid-beta, ApoA-II, human cystatin C and stefin B as model proteins. We prepared enzymatic lipophilized/glycosylated phenolic compounds in addition to mono- and di-catecholates of sesamin, and used for anti-amyloidal experiments. As the result, we found that there was a strong relationship between amphiphilicity and anti-amyloidal activity of tested phenolic compounds. We also found that lipophilic chain length introduced was an important factor in the anti-amyloidal activity of novel catechol derivatives.