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Updated: May 29, 2026

Bridging the Bio-Electronic Interface with Biofabrication
Published on: June 6, 2012
Graphene oxide as an enzyme inhibitor: modulation of activity of α-chymotrypsin
Mrinmoy De1, Stanley S Chou, Vinayak P Dravid
1Department of Materials Science and Engineering, International Institute for Nanotechnology, Northwestern University, Evanston, Illinois 60208, United States. m-de@northwestern.edu
Abstract:
We have investigated the efficacy of graphene oxide (GO) in modulating enzymatic activity. Specifically, we have shown that GO can act as an artificial receptor and inhibit the activity of α-chymotrypsin (ChT), a serine protease. Most significantly, our data demonstrate that GO exhibits the highest inhibition dose response (by weight) for ChT inhibition compared with all other reported artificial inhibitors. Through fluorescence spectroscopy and circular dichroism studies, we have shown that this protein-receptor interaction is highly biocompatible and conserves the protein's secondary structure over extended periods (>24 h). We have also explored GO-enzyme interactions by controlling the ionic strength of the medium, which attenuates the host-guest electrostatic interactions. These findings suggest a new generation of enzymatic inhibitors that can be applied to other complex proteins by systematic modification of the GO functionality.
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