Issue 18, 2018

Covalent functionalization of graphene oxide with d-mannose: evaluating the hemolytic effect and protein corona formation

Abstract

In this work, graphene oxide (GO) was covalently functionalized with D-mannose (man-GO) using mannosylated ethylenediamine. XPS (C1s and N1s) confirmed the functionalization of GO through the binding energies at 288.2 eV and 399.8 eV, respectively, which are attributed to the amide bond. ATR-FTIR spectroscopy showed an increase in the amine bond intensity, at 1625 cm−1 (stretching C[double bond, length as m-dash]O), after the functionalization step. Furthermore, the man-GO toxicity to human red blood cells (hemolysis) and its nanobiointeractions with human plasma proteins (hard corona formation) were evaluated. The mannosylation of GO drastically reduced its toxicity to red blood cells. SDS-PAGE analysis showed that the mannosylation process of GO also drastically reduced the amount of the proteins in the hard corona. Additionally, proteomics analysis by LC–MS/MS revealed 109 proteins in the composition of the man-GO hard corona. Finally, this work contributes to future biomedical applications of graphene-based materials functionalized with active biomolecules.

Graphical abstract: Covalent functionalization of graphene oxide with d-mannose: evaluating the hemolytic effect and protein corona formation

Supplementary files

Article information

Article type
Paper
Submitted
16 nov 2017
Accepted
08 apr 2018
First published
10 apr 2018

J. Mater. Chem. B, 2018,6, 2803-2812

Covalent functionalization of graphene oxide with D-mannose: evaluating the hemolytic effect and protein corona formation

M. de Sousa, C. H. Z. Martins, L. S. Franqui, L. C. Fonseca, F. S. Delite, E. M. Lanzoni, D. S. T. Martinez and O. L. Alves, J. Mater. Chem. B, 2018, 6, 2803 DOI: 10.1039/C7TB02997G

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements