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• W2013752458 abstract "The trpzip peptides are small, monomeric, and extremely stable β-hairpins that have become valuable tools for studying protein folding. Here, we show that trpzip-3 inhibits aggregation in two very different amyloid systems: transthyretin and Aβ(1–42). Interestingly, Trp → Leu mutations renders the peptide ineffective against transthyretin, but Aβ inhibition remains. Computational docking was used to predict the interactions between trpzip-3 and transthyretin, suggesting that inhibition occurs via binding to the outer region of the thyroxine-binding site, which is supported by dye displacement experiments." @default.
• W2013752458 created "2016-06-24" @default.
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• W2013752458 date "2013-08-05" @default.
• W2013752458 modified "2023-09-23" @default.
• W2013752458 title "Designed Trpzip-3 β-Hairpin Inhibits Amyloid Formation in Two Different Amyloid Systems" @default.
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• W2013752458 doi "https://doi.org/10.1021/ml300478w" @default.
• W2013752458 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4027462" @default.
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