Peptide sequence-driven direct electron transfer properties and binding behaviors of gold-binding peptide-fused glucose dehydrogenase on electrode

Oriented enzyme immobilization on electrodes is crucial for interfacial electrical coupling of direct electron transfer (DET)-based enzyme-electrode systems. As inorganic-binding peptides are introduced as molecular binders and enzyme-orienting agents, inorganic-binding peptide-fused enzymes should be designed and constructed to achieve efficient DET. In this study, it is aimed to compare the effects of various gold-binding peptides (GBPs) fused to enzymes on electrocatalytic activity, bioactivity, and material-binding behaviors. Here, GBPs with identical gold-binding properties but different amino acid sequences were fused to the FAD-dependent glucose dehydrogenase gamma- alpha complex (GDH gamma alpha) to generate four GDH gamma alpha variants. The structural, biochemical, mechanical, and bioelectrochemical properties of these GDH gamma alpha variants immobilized on electrode were determined by their fused GBPs. Our results confirmed that the GBP type is vital in the design, construction, and optimization of GBP-fused enzyme-modified electrodes for facile interfacial DET and practical DET-based enzyme-electrode systems.

Automated summary

This study compared the effects of different gold-binding peptides fused to enzymes on electrocatalytic activity, bioactivity, and material-binding behaviors, demonstrating the vital role of GBP type in the design, construction, and optimization of enzyme-modified electrodes for efficient interfacial DET in DET-based enzyme-electrode systems.