Preorganization boosts the artificial esterase activity of a self-assembling peptide

The creation of artificial enzymes to mimic natural enzymes remains a great challenge owing to the complexity of the structural arrangement of the essential amino acids in catalytic centers. In this study, we used the phosphatase-based enzyme-instructed self-assembly (EISA) to supervise artificial esterases' final structures and catalytic activities. We reported that peptide precursors containing different phosphorylation sites could preorganize into alternated nanostructures and undergo dephosphorylation in the presence of alkaline phosphatase (ALP) with variation in kinetic and thermodynamic profiles. Although identical self-assembly compositions were formed after dephosphorylation, precursors with more enhanced preorganized states tended to better promote ALP dephosphorylation, facilitate further self-assembly, and strengthen the catalytic activities of the final assemblies. We envisioned that our strategy would be useful for further construction and manipulation of various artificial enzymes with superior catalytic activities.

Automated summary

In this study, the researchers used phosphatase-based enzyme-instructed self-assembly to monitor the final structures and catalytic activities of artificial esterases. Peptide precursors with different phosphorylation sites could preorganize into alternating nanostructures and undergo dephosphorylation in the presence of alkaline phosphatase. Predecessors with enhanced preorganized states were more effective in promoting dephosphorylation and enhancing catalytic activities.