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Synthesis of polyethylenimine modified Fe3O4 nanoparticles immobilized Cu2+ for highly efficient proteins adsorption
Alternative TitleColloid Surf. A-Physicochem. Eng. Asp.
Xia, Tingting1; Guan, Yueping1; Yang, Mingzhu1; Xiong, Wubin1; Wang, Ning2; Zhao, Shen1; Guo, Chen2
2014-02-20
Source PublicationCOLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS
ISSN0927-7757
Volume443Issue:FEB.Pages:552-559
AbstractWe report the modification of amine-functioned Fe3O4 nanoparticles (provided by the Laboratory of BioMedical Materials of University of Science and Technology Beijing) with polyethylenimine (PEI) using glutaraldehyde (GA) as a linker to increase the concentration of primary amine groups on the surface. The resultant Fe3O4-PEI NPs with immobilized iminodiacetic acid (IDA)-Cu2+ groups were applied to investigate the adsorption capacity and selectivity of model proteins: bovine hemoglobin (BHb) and bovine serum albumin (BSA). The Fe3O4-PEI NPs were characterized by transmission electron microscopy (TEM), vibrating sample magnetometer (VSM), particle analyzer, attenuated total reflection-Fourier transform infrared spectroscopy (ATR-FTIR), ninhydrin colorimetry and thermogravimetric analysis (TGA). The results showed that the well dispersed Fe3O4-PEI NPs had an average size of 172.6 nm and were superparamagnetic with saturation magnetization of 71.11 emu/g. The characteristic peaks of PEI appeared in the ATR-FTIR spectra of Fe3O4-PEI NPs. The study of zeta potential measurement presented that the isoelectric points of the Fe3O4-PEI NPs increased to 10.5. Ninhydrin colorimetry analysis of primary amine groups showed that the concentration of primary amine groups on the surface of Fe3O4-PEI NPs increased to 0.45 mmol/g and that of TGA is 0.53 mmol/g. These results showed that PEI had been successfully modified on the surface of amine-functioned Fe3O4 NPs and the concentration of primary amine groups was significantly increased. The analysis of protein adsorption indicated that the adsorption capacity of BHb was up to about 6000 mg/g and that of BSA was only about 2000 mg/g, which was about one third of that of BHb. The research on the selectivity of protein adsorption was conducted by HPLC. The result showed that the adsorption capacity of BHb was 2.5 times as high as that of BSA, which further proved Fe3O4-PEI-Cu2+ NPs shows specific adsorption for proteins. These properties suggested the potential of the Fe3O4-PEI-Cu2+ NPs as protein adsorbent. (C) 2013 Elsevier B.V. All rights reserved.; We report the modification of amine-functioned Fe3O4 nanoparticles (provided by the Laboratory of BioMedical Materials of University of Science and Technology Beijing) with polyethylenimine (PEI) using glutaraldehyde (GA) as a linker to increase the concentration of primary amine groups on the surface. The resultant Fe3O4-PEI NPs with immobilized iminodiacetic acid (IDA)-Cu2+ groups were applied to investigate the adsorption capacity and selectivity of model proteins: bovine hemoglobin (BHb) and bovine serum albumin (BSA). The Fe3O4-PEI NPs were characterized by transmission electron microscopy (TEM), vibrating sample magnetometer (VSM), particle analyzer, attenuated total reflection-Fourier transform infrared spectroscopy (ATR-FTIR), ninhydrin colorimetry and thermogravimetric analysis (TGA). The results showed that the well dispersed Fe3O4-PEI NPs had an average size of 172.6 nm and were superparamagnetic with saturation magnetization of 71.11 emu/g. The characteristic peaks of PEI appeared in the ATR-FTIR spectra of Fe3O4-PEI NPs. The study of zeta potential measurement presented that the isoelectric points of the Fe3O4-PEI NPs increased to 10.5. Ninhydrin colorimetry analysis of primary amine groups showed that the concentration of primary amine groups on the surface of Fe3O4-PEI NPs increased to 0.45 mmol/g and that of TGA is 0.53 mmol/g. These results showed that PEI had been successfully modified on the surface of amine-functioned Fe3O4 NPs and the concentration of primary amine groups was significantly increased. The analysis of protein adsorption indicated that the adsorption capacity of BHb was up to about 6000 mg/g and that of BSA was only about 2000 mg/g, which was about one third of that of BHb. The research on the selectivity of protein adsorption was conducted by HPLC. The result showed that the adsorption capacity of BHb was 2.5 times as high as that of BSA, which further proved Fe3O4-PEI-Cu2+ NPs shows specific adsorption for proteins. These properties suggested the potential of the Fe3O4-PEI-Cu2+ NPs as protein adsorbent. (C) 2013 Elsevier B.V. All rights reserved.
KeywordFe3o4-pei Nps Protein Adsorption Bhb Bsa Adsorption Capacity Selectivity
SubtypeArticle
WOS HeadingsScience & Technology ; Physical Sciences
DOI10.1016/j.colsurfa.2013.12.026
URL查看原文
Indexed BySCI
Language英语
WOS KeywordCOMPOSITE NANOPARTICLES ; AFFINITY LIGANDS ; PURIFICATION ; SEPARATION ; POLYMERIZATION ; MICROSPHERES ; SUPPORTS ; ENZYMES ; BEADS ; ACID
WOS Research AreaChemistry
WOS SubjectChemistry, Physical
WOS IDWOS:000342501300076
Citation statistics
Cited Times:32[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Version出版稿
Identifierhttp://ir.ipe.ac.cn/handle/122111/11660
Collection研究所(批量导入)
Affiliation1.Univ Sci & Technol Beijing, Sch Mat Sci & Engn, Beijing 100083, Peoples R China
2.Chinese Acad Sci, Inst Proc Engn, Lab Separat Sci & Engn, State Key Lab Biochem Engn, Beijing 100190, Peoples R China
Recommended Citation
GB/T 7714
Xia, Tingting,Guan, Yueping,Yang, Mingzhu,et al. Synthesis of polyethylenimine modified Fe3O4 nanoparticles immobilized Cu2+ for highly efficient proteins adsorption[J]. COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS,2014,443(FEB.):552-559.
APA Xia, Tingting.,Guan, Yueping.,Yang, Mingzhu.,Xiong, Wubin.,Wang, Ning.,...&Guo, Chen.(2014).Synthesis of polyethylenimine modified Fe3O4 nanoparticles immobilized Cu2+ for highly efficient proteins adsorption.COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS,443(FEB.),552-559.
MLA Xia, Tingting,et al."Synthesis of polyethylenimine modified Fe3O4 nanoparticles immobilized Cu2+ for highly efficient proteins adsorption".COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS 443.FEB.(2014):552-559.
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