Enhanced enrichment performance of nickel oxide nanoparticles via fabrication of a nanocomposite with a graphene template

Fatima, Batool, Jabeen, Fahmida, Padashbarmchi, Zahra and Najam-Ul-Haq, Muhammad (2015) Enhanced enrichment performance of nickel oxide nanoparticles via fabrication of a nanocomposite with a graphene template. RSC Advances, 5 30: 23658-23665. doi:10.1039/c4ra17299j


Author Fatima, Batool
Jabeen, Fahmida
Padashbarmchi, Zahra
Najam-Ul-Haq, Muhammad
Title Enhanced enrichment performance of nickel oxide nanoparticles via fabrication of a nanocomposite with a graphene template
Journal name RSC Advances   Check publisher's open access policy
ISSN 2046-2069
Publication date 2015-01-01
Year available 2015
Sub-type Article (original research)
DOI 10.1039/c4ra17299j
Open Access Status Not Open Access
Volume 5
Issue 30
Start page 23658
End page 23665
Total pages 8
Place of publication Cambridge, United Kingdom
Publisher Royal Society of Chemistry
Collection year 2016
Language eng
Formatted abstract
Metal oxide based nanocomposites are applied in phosphoproteomics for enrichment through the surface hydroxyl groups of metal oxides, though the role of the metal is rarely described. Using graphene as a template after modification with nickel oxide, a nanocomposite with an increased surface area is fabricated and applied to phosphopeptides. Characterisation shows a narrow size distribution of 15–20 nm, BET surface area of 179.70 m2 g-1 and a pore volume of 0.44 cm3 g-1. The graphene possesses well distributed NiO nanoparticles showing selectivity up to 1000 folds of complexity with a sensitivity as low as 1 femtomole. The G–NiO nanocomposite shows a higher selectivity towards phosphopeptides compared to TiO2, ZrO2 and NiO nanoparticles. Theenrichment with the G–NiO nanocomposite is tested for biological samples like egg yolk, non-fat milk and human serum. Phosphopeptides having phosphorylations of up to 6 phosphate groups, derived from phosvitin and lipovitellin, are enriched in the egg yolk digest. Phosphopeptides characteristic of casein variants are enriched in the non-fat milk digest with a recovery of aS1 21.9%, aS2 30% and b-casein 20%. Phosphorylated proteins are identified in human serum through the enrichment of phosphopeptides.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
Australian Institute for Bioengineering and Nanotechnology Publications
 
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