Journal
ACS MEDICINAL CHEMISTRY LETTERS
Volume 4, Issue 9, Pages 824-828Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ml300478w
Keywords
Alzheimer's disease; Trpzip; transthyretin; ANS fluorescence; computational docking
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Funding
- W. H. Coulter Foundation Translational Research Partnership Program
- National Science Foundation [CBET-0966977]
- Coins for Alzheimer's Research Trust
- Intramural Research Program of the NIAID
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The trpzip peptides are small, monomeric, and extremely stable beta-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 A beta(1-42). Interestingly, Trp -> Leu mutations renders the peptide ineffective against transthyretin, but A beta 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.
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