Supramolecule self-assembly synthesis of amyloid phenylalanine-Cu fibrils with laccase-like activity and their application for dopamine determination.

Laccases are multicopper proteins for dioxygen-involved oxidation of a broad spectrum of organic compounds. I Novel amyloid-like phenylalanine-Cu (F-Cu(II)) fibrils were developed, which were obtained via supramolecular self-assembly of Cu and phenylalanine (F) under basic condition. The obtained amyloid-like fibrils represented highly periodic structure, of which the lattice unit was constructed via alternating hydrophobic (aromatic environment) and hydrophilic (both hydrogen bonding and Cu(II) coordination) interactions. Relative to natural laccases, the amyloid-like F-Cu(II) architecture exhibited comparable substrate affinity (Michaelis constant, K = 0.75 mM) and higher catalytic efficiency (k/K = 773.33 × 10 g minL). Moreover, it exhibited remarkable tolerances in pH (4 ~ 10), temperature (room temperature ~ 200 ℃), organic solvent, and long-term storage (> 15 days). These stabilities were superior among the reported nature and artificial laccases, presenting a more promising candidate in various chemo- or bio-applications. In addition, F-Cu(II) fibrils could catalyze the oxidation of dopamine (DA) to a brown product, in which a new absorption band at 470 nm was observed. Based on this, a simple colorimetric assay for the detection of DA could be performed. We reported a novel amyloid-like phenylalanine-Cu fibrils, in which F-Cu complex can mimick the T1 site of natural laccase to oxidize the substrates. Then electrons transferred to F-Cu complex via N-H···O=C hydrogen binding pathway. Finally, the dioxygen was transformed to water though radical reaction.