Graphene oxide as an enzyme inhibitor: Modulation of activity of α-chymotrypsin

Mrinmoy De*, Stanley S. Chou, Vinayak P. Dravid

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

136 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)17524-17527
Number of pages4
JournalJournal of the American Chemical Society
Volume133
Issue number44
DOIs
StatePublished - Nov 9 2011

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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