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Issue 18, 2015
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Molecular effects of encapsulation of glucose oxidase dimer by graphene

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Abstract

Knowing the nature of the enzyme–graphene interface is critical for a design of graphene-based biosensors. Extensive contacts between graphene and enzyme could be obtained by employing a suitable encapsulation which does not impede its enzymatic reaction. We have performed molecular dynamics simulations to obtain an insight on many forms of contact between glucose oxidase dimer and the single-layer graphene nano-sheets. The unconnected graphene sheets tended to form a flat stack regardless of their initial positions around the enzyme, whereas the same graphene sheets linked together formed a flower-like shape engendering different forms of wrapping of the enzyme. During the encapsulation no core hydrophobic residues of the enzyme were exposed. Since the polar and charged amino acids populated the enzyme's surface we also estimated, using DFT calculations, the interaction energies of individual polar and charged amino acid residues with graphene. It was found that the negatively charged residues can bind to graphene unexpectedly strongly; however, the main effect of encapsulation comes from the overlap of adjacent edges of graphene sheets.

Graphical abstract: Molecular effects of encapsulation of glucose oxidase dimer by graphene

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Supplementary files

Article information


Submitted
22 Dec 2014
Accepted
16 Jan 2015
First published
16 Jan 2015

RSC Adv., 2015,5, 13570-13578
Article type
Paper
Author version available

Molecular effects of encapsulation of glucose oxidase dimer by graphene

U. Ghoshdastider, R. Wu, B. Trzaskowski, K. Mlynarczyk, P. Miszta, M. Gurusaran, S. Viswanathan, V. Renugopalakrishnan and S. Filipek, RSC Adv., 2015, 5, 13570
DOI: 10.1039/C4RA16852F

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