Spectroscopic investigation on the binding interactions between graphene quantum dots and carbonic anhydrase

As a new member of the nanomaterials family, ultrasmall graphene quantum dots (GQDs) have shown broad application prospects in the field of biomedicine, but the analysis of their biological effects at the molecular level is yet limited. Herein, carbonic anhydrase (CA) was selected as a model protein to assess the interactions between GQDs and biomacromolecules. A range of spectroscopic techniques were employed to systematically investigate the binding interactions between GQDs and CA and the catalytic function of CA in the presence of GQDs was evaluated. Experimental results showed that GQDs could quench the intrinsic fluorescence of CA and the concentration dependent quenching efficiency exhibited an obvious deviation from the linear plot, indicating a static binding mode. Further investigation suggested that van der Waal interactions and hydrogen bonding were the main driving forces. Additionally, circular dichroism measurement showed that the binding of GQDs induced slight conformational changes of CA. The catalytic capability assessment proved that these binding interactions resulted in the reduction of the biological functions of CA. This comprehensive study provided important insight into the interaction of GQDs with biomacromolecules, which would be crucial for the further applications of GQDs and other nanomaterials in the biomedical field. CO 2021 Elsevier B.V. All rights reserved.

Automated summary

This study systematically investigated the interactions between ultrasmall graphene quantum dots (GQDs) and biomacromolecules using carbonic anhydrase (CA) as a model protein. The results showed that GQDs could quench the intrinsic fluorescence of CA in a static binding mode driven by van der Waal interactions and hydrogen bonding. Additionally, the binding of GQDs induced slight conformational changes of CA and resulted in the reduction of its biological functions.