Carbon dots with chiral surface selectively inhibit the activity of laccase

Chiral carbon dots (CDots) have received much attention in biocatalysis due to their biocompatibility and low toxicity. For chiral CDots-enzyme hybrid system, great efforts are needed to understand the interactions between chiral CDots and enzymes. Here, chiral CDots (L-/D-Trp-CDots) from citric acid and L-/D-tryptophan were designed and synthesized. The obtained L-Trp-CDots were used to regulate the activity of laccase, showing an 87.26 % inhibition rate of laccase, which is significantly higher than that of D-Trp-CDots (57.84 %) under the same reaction conditions. It is chiral functional groups rather than the carbon core play the important role in chiral CDots for regulating enzymatic activity in this system.