ArticleScientific reports2016
Modulation of Protein Fouling and Interfacial Properties at Carbon Surfaces via Immobilization of Glycans Using Aryldiazonium Chemistry.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Influence of surface chemistry and morphology of nanoparticles on protein corona formation.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2022Review
- Controlling the Carbon-Bio Interface via Glycan Functional Adlayers for Applications in Microbial Fuel Cell Bioanodes.Molecules (Basel, Switzerland) · 2021Article
- Assessing Surface Coverage of Aminophenyl Bonding Sites on Diazotised Glassy Carbon Electrodes for Optimised Electrochemical Biosensor Performance.Nanomaterials (Basel, Switzerland) · 2021Article
- Capacitive storage at nitrogen doped amorphous carbon electrodes: structural and chemical effects of nitrogen incorporation.RSC advances · 2019Article
- Unbiased biocatalytic solar-to-chemical conversion by FeOOH/BiVONature communications · 2018Article
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Authors and funding
8 authors.
Funding
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Abstract
Carbon materials and nanomaterials are of great interest for biological applications such as implantable devices and nanoparticle vectors, however, to realize their potential it is critical to control formation and composition of the protein corona in biological media. In this work, protein adsorption studies were carried out at carbon surfaces functionalized with aryldiazonium layers bearing mono- and di-saccharide glycosides. Surface IR reflectance absorption spectroscopy and quartz crystal microbalance were used to study adsorption of albumin, lysozyme and fibrinogen. Protein adsorption was found to decrease by 30-90% with respect to bare carbon surfaces; notably, enhanced rejection was observed in the case of the tested di-saccharide vs. simple mono-saccharides for near-physiological protein concentration values. ζ-potential measurements revealed that aryldiazonium chemistry results in the immobilization of phenylglycosides without a change in surface charge density, which is known to be important for protein adsorption. Multisolvent contact angle measurements were used to calculate surface free energy and acid-base polar components of bare and modified surfaces based on the van Oss-Chaudhury-Good model: results indicate that protein resistance in these phenylglycoside layers correlates positively with wetting behavior and Lewis basicity.
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