Designed Trpzip‑3 β‑Hairpin Inhibits
Amyloid Formation in Two Different Amyloid Systems
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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