Transthyretin tetramers dissociate into monomers that aggregate to form toxic oligomers and fibrils in several amyloid diseases. Elucidating the structure of these aggregates is critical to understanding these and other amyloid diseases. This presentation describes the X-ray crystallographic structure of a β-hairpin peptide derived from a region of TTR that is important in aggregation, TTR<sub>106-121</sub>. The peptide crystallizes to form square hydrophobic channels that have not previously been observed. The design, structure, and assembly of the TTR-derived peptide will be described and the implications for amyloid diseases will be discussed.

β-hairpin peptide derived from transthyretin 106-121 that forms square hydrophobic channels

251st National Meeting (2016)

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