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Issue 5, 2020
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Modulation of protein–graphene oxide interactions with varying degrees of oxidation

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Abstract

The degree of oxidation of graphene oxide (GO) has been shown to be important for its toxicity and drug-loading efficiency. However, the effect of its variations on GO–protein interaction remains unclear. Here, we evaluate the effect of the different oxidation degrees of GO on its interaction with human ubiquitin (8.6 kDa) using solution state nuclear magnetic resonance (NMR) spectroscopy in combination with other biophysical techniques. Our findings show that the interaction between the protein and the different GO samples is weak and electrostatic in nature. It involves fast dynamic exchange of the protein molecules from the surface of the GO. As the oxidation degree of the GO increases, the extent of the interaction with the protein changes. The interaction of the protein with GO can thus be modulated by tuning the degree of oxidation. This study opens up new avenues to design appropriate graphenic materials for use in various biomedical fields such as drug delivery, biomedical devices and imaging.

Graphical abstract: Modulation of protein–graphene oxide interactions with varying degrees of oxidation

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Supplementary files

Article information


Submitted
28 Dec 2019
Accepted
22 Mar 2020
First published
27 Mar 2020

This article is Open Access

Nanoscale Adv., 2020,2, 1904-1912
Article type
Paper

Modulation of protein–graphene oxide interactions with varying degrees of oxidation

S. A. Malik, Z. Mohanta, C. Srivastava and H. S. Atreya, Nanoscale Adv., 2020, 2, 1904
DOI: 10.1039/C9NA00807A

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    [Original citation] - Published by The Royal Society of Chemistry.

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