Synthesis of a hydrophilic maltose functionalized Au NP/PDA/FeO-RGO magnetic nanocomposite for the highly specific enrichment of glycopeptides
The development of methods to isolate and enrich low-abundance glycopeptides is an important prerequisite for glycoproteomics research. In this study, a hydrophilic maltose functionalized Au nanoparticle (NP)/polydopamine (PDA)/Fe 3 O 4 -reduced graphene oxide (RGO) nanocomposite has been successful...
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Published in | RSC advances Vol. 5; no. 73; pp. 5948 - 59416 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
08.07.2015
|
Online Access | Get full text |
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Summary: | The development of methods to isolate and enrich low-abundance glycopeptides is an important prerequisite for glycoproteomics research. In this study, a hydrophilic maltose functionalized Au nanoparticle (NP)/polydopamine (PDA)/Fe
3
O
4
-reduced graphene oxide (RGO) nanocomposite has been successfully synthesized in mild conditions. The bioadhesive polydopamine film was prepared by self-polymerization on the surface of Fe
3
O
4
-graphene oxide, which not only prevents the agglomeration of the graphene sheets and enhances the specific surface area, but also facilitates the Au NP immobilization. A great number of loading Au NPs possess the highly available surface area for the immobilization of the high density of the thiol-terminated maltose
via
Au-S bonds. The resulting Au NP-maltose/PDA/Fe
3
O
4
-RGO nanocomposite exhibits excellent environmental stability, good biocompatibility and water dispersibility. Furthermore, the highly loaded Fe
3
O
4
NPs make the enrichment very convenient. With all of these advances, the novel Au NP-maltose/PDA/Fe
3
O
4
-RGO nanocomposite presents selective enrichment of the glycopeptides from a low concentration of horseradish peroxidase tryptic digest (0.1 ng μL
−1
).
A novel approach was developed to synthesize a hydrophilic thiol-terminated maltose-functionalized Au NP/PDA/Fe
3
O
4
-RGO nanocomposite which exhibited high selectivity and detection sensitivity in the enrichment of glycopeptides from complex samples. |
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ISSN: | 2046-2069 |
DOI: | 10.1039/c5ra06911d |