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 SurfacesAutor(es)
Fecha
2020-01-06Cita bibliográfica
Juan Pedro Merino et al 2020 2D Mater. 7 024003
Resumen
[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.
Palabras clave
Graphene
CVD
Chemical modification
LDI
Mass spectrometry
Carbohydrate microarrays
Lectin
CVD
Chemical modification
LDI
Mass spectrometry
Carbohydrate microarrays
Lectin
Versión del editor
Derechos
© 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