“…Peptide IHIHIQI was the most active sequence and has served as template to develop many other catalytic amyloids. ,,− Amyloid activities include hydrolysis of ester and phosphoester bonds, redox reactions, and retro aldol condensations, among others. , Based on the active site of nucleotide-processing enzymes, we have developed catalytic amyloids carrying active aspartate groups (Asp). , These catalytic amyloids exhibit manganese-dependent hydrolytic activity that specifically cleaves the phosphoanhydride bonds of adenosine triphosphate (ATP) and other nucleotides. Most catalytic amyloids rely on metal ions for their activity. , It is known that divalent metals can influence the aggregation of different (noncatalytic) pathological amyloids. − Herein, we show that biologically relevant metal ions can guide the assembly of a small peptide into metal-specific aggregation kinetics and morphologies. All tested ions triggered the conformational transition to the amyloid state, but only manganese induced hydrolytic activity.…”