Mass Spectrometry of Carbohydrate-Protein Interactions on a Glycan Array Conjugated to CVD Graphene Surfaces
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Mass Spectrometry of Carbohydrate-Protein Interactions on a Glycan Array Conjugated to CVD Graphene SurfacesAuthor(s)
Date
2020-01-06Citation
Juan Pedro Merino et al 2020 2D Mater. 7 024003
Abstract
[Abstract]: Mass spectrometry (MS) is a valuable tool for functional genomic, proteomic, and glycomic studies. In particular, the combination of MS with microarrays is a powerful technique for analyzing the activity of carbohydrate processing enzymes and for the identification of car-bohydrate-binding proteins (lectins) in complex matrices. On the other hand, graphene exhi-bits high desorption/ionization efficiency, good conductivity and optical transparency, specifi-cations of a high-performance component for matrix-assisted laser desorption/ionization (MALDI) platforms. Besides, the chemical functionalization of graphene increases the adsor-ption capability of functional biomolecules (e.g. receptors), resulting in very stable interfaces. Taking advantage of the properties of graphene, we developed several modified chemical vapor deposited graphene (CVDG)-based glycan arrays on different substrates including ITO and bare glass, as a potential sensing platform for carbohydrate-lectin interactions, which are involved in a plethora of biological processes. The glycan arrays were fully characterized by MALDI-MS analysis and, in some cases, optical microscopy.
Keywords
Graphene
CVD
Chemical modification
LDI
Mass spectrometry
Carbohydrate microarrays
Lectin
CVD
Chemical modification
LDI
Mass spectrometry
Carbohydrate microarrays
Lectin
Editor version
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© 2020 IOP Publishing Ltd. Original content from this work may be used under the terms of the Creative Commons Attribution 3.0 licence (http://creativecommons.org/licenses/by/3.0). Any further distribution of this work must maintain attribution to the author(s) and the title of the work, journal citation and DOI.
ISSN
2053-1583