Amyloid peptide hydrogels via formation of coordination polymers with Ag+ by its core peptide equipped with a C-cysteine.

We report that the core sequence of amyloid ß (Aß) peptide, KLVFF, when equipped with a C-terminal cysteine residue, exhibited an extremely low minimum hydrogelation concentration of 0.05 wt% in the presence of Ag+ in pH 5 buffer, with this concentration 2 orders of magnitude lower than that of the pentapeptide itself. The CD signal of the Ag+-L-KLVFFC hydrogel was observed to be sensitive to the early-stage aggregation of amyloid ß peptide.