Surface modification and bioconjugation of FeCo magnetic nanoparticles with proteins

Wei Wang; Ying Jing; Shihai He; Jian Ping Wang; Jian Ping Zhai

doi:10.1016/j.colsurfb.2013.11.050

Surface modification and bioconjugation of FeCo magnetic nanoparticles with proteins

Wei Wang, Ying Jing, Shihai He, Jian Ping Wang, Jian Ping Zhai

Electrical and Computer Engineering

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

Abstract

Magnetic Fe₇₀Co₃₀ nanoparticles with a cubic shape and a mean size of 15±1.5nm were fabricated using a magnetron-sputtering-based gas phase condensation deposition method. The particles had a high saturation magnetization of 220emu/g, which is much higher than that of commercially available iron oxide nanoparticles. The FeCo nanoparticles were modified by 3-aminopropyltriethoxy silane and subsequently activated by glutaraldehyde, leading to successful attachment of aldehyde groups onto nanoparticle surfaces. Three proteins, namely streptavidin, PAPP-A antibody and Nectin-4 antibody, were immobilized on glutaraldehyde activated FeCo nanoparticles, and their loading levels were quantitatively evaluated. Our results show that loading capabilities are 95μg of streptavidin, 128μg of PAPP-A, and 125μg of Nectin-4 antibody per milligram of FeCo nanoparticles, and that the three immobilized proteins retain their binding bioactivity. The protein-FeCo conjugates may find valuable applications involving magnetic separation and purification of proteins and cells, and the magnetic detection of biomolecules.

Original language	English (US)
Pages (from-to)	449-456
Number of pages	8
Journal	Colloids and Surfaces B: Biointerfaces
Volume	117
DOIs	https://doi.org/10.1016/j.colsurfb.2013.11.050
State	Published - May 1 2014

Bibliographical note

Funding Information:
This work was supported by the GMR Innovation Grant through the Office for Technology Commercialization, University of Minnesota. Parts of this work were carried out in the Characterization Facility, University of Minnesota, which receives partial support from NSF through the MRSEC program. Wei Wang also acknowledges the financial support from China Scholarship Council.

Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.

Keywords

FeCo magnetic nanoparticles
Immobilization
Protein
Surface modification

Access

10.1016/j.colsurfb.2013.11.050

OpenUrl availability

Full text

Cite this

@article{60d14b4aa202497ba4d87fa467219d97,

title = "Surface modification and bioconjugation of FeCo magnetic nanoparticles with proteins",

abstract = "Magnetic Fe70Co30 nanoparticles with a cubic shape and a mean size of 15±1.5nm were fabricated using a magnetron-sputtering-based gas phase condensation deposition method. The particles had a high saturation magnetization of 220emu/g, which is much higher than that of commercially available iron oxide nanoparticles. The FeCo nanoparticles were modified by 3-aminopropyltriethoxy silane and subsequently activated by glutaraldehyde, leading to successful attachment of aldehyde groups onto nanoparticle surfaces. Three proteins, namely streptavidin, PAPP-A antibody and Nectin-4 antibody, were immobilized on glutaraldehyde activated FeCo nanoparticles, and their loading levels were quantitatively evaluated. Our results show that loading capabilities are 95μg of streptavidin, 128μg of PAPP-A, and 125μg of Nectin-4 antibody per milligram of FeCo nanoparticles, and that the three immobilized proteins retain their binding bioactivity. The protein-FeCo conjugates may find valuable applications involving magnetic separation and purification of proteins and cells, and the magnetic detection of biomolecules.",

keywords = "FeCo magnetic nanoparticles, Immobilization, Protein, Surface modification",

author = "Wei Wang and Ying Jing and Shihai He and Wang, {Jian Ping} and Zhai, {Jian Ping}",

note = "Funding Information: This work was supported by the GMR Innovation Grant through the Office for Technology Commercialization, University of Minnesota. Parts of this work were carried out in the Characterization Facility, University of Minnesota, which receives partial support from NSF through the MRSEC program. Wei Wang also acknowledges the financial support from China Scholarship Council. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",

year = "2014",

month = may,

day = "1",

doi = "10.1016/j.colsurfb.2013.11.050",

language = "English (US)",

volume = "117",

pages = "449--456",

journal = "Colloids and Surfaces B: Biointerfaces",

issn = "0927-7765",

publisher = "Elsevier",

}

TY - JOUR

T1 - Surface modification and bioconjugation of FeCo magnetic nanoparticles with proteins

AU - Wang, Wei

AU - Jing, Ying

AU - He, Shihai

AU - Wang, Jian Ping

AU - Zhai, Jian Ping

N1 - Funding Information: This work was supported by the GMR Innovation Grant through the Office for Technology Commercialization, University of Minnesota. Parts of this work were carried out in the Characterization Facility, University of Minnesota, which receives partial support from NSF through the MRSEC program. Wei Wang also acknowledges the financial support from China Scholarship Council. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.

PY - 2014/5/1

Y1 - 2014/5/1

N2 - Magnetic Fe70Co30 nanoparticles with a cubic shape and a mean size of 15±1.5nm were fabricated using a magnetron-sputtering-based gas phase condensation deposition method. The particles had a high saturation magnetization of 220emu/g, which is much higher than that of commercially available iron oxide nanoparticles. The FeCo nanoparticles were modified by 3-aminopropyltriethoxy silane and subsequently activated by glutaraldehyde, leading to successful attachment of aldehyde groups onto nanoparticle surfaces. Three proteins, namely streptavidin, PAPP-A antibody and Nectin-4 antibody, were immobilized on glutaraldehyde activated FeCo nanoparticles, and their loading levels were quantitatively evaluated. Our results show that loading capabilities are 95μg of streptavidin, 128μg of PAPP-A, and 125μg of Nectin-4 antibody per milligram of FeCo nanoparticles, and that the three immobilized proteins retain their binding bioactivity. The protein-FeCo conjugates may find valuable applications involving magnetic separation and purification of proteins and cells, and the magnetic detection of biomolecules.

AB - Magnetic Fe70Co30 nanoparticles with a cubic shape and a mean size of 15±1.5nm were fabricated using a magnetron-sputtering-based gas phase condensation deposition method. The particles had a high saturation magnetization of 220emu/g, which is much higher than that of commercially available iron oxide nanoparticles. The FeCo nanoparticles were modified by 3-aminopropyltriethoxy silane and subsequently activated by glutaraldehyde, leading to successful attachment of aldehyde groups onto nanoparticle surfaces. Three proteins, namely streptavidin, PAPP-A antibody and Nectin-4 antibody, were immobilized on glutaraldehyde activated FeCo nanoparticles, and their loading levels were quantitatively evaluated. Our results show that loading capabilities are 95μg of streptavidin, 128μg of PAPP-A, and 125μg of Nectin-4 antibody per milligram of FeCo nanoparticles, and that the three immobilized proteins retain their binding bioactivity. The protein-FeCo conjugates may find valuable applications involving magnetic separation and purification of proteins and cells, and the magnetic detection of biomolecules.

KW - FeCo magnetic nanoparticles

KW - Immobilization

KW - Protein

KW - Surface modification

UR - http://www.scopus.com/inward/record.url?scp=84899621071&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84899621071&partnerID=8YFLogxK

U2 - 10.1016/j.colsurfb.2013.11.050

DO - 10.1016/j.colsurfb.2013.11.050

M3 - Article

C2 - 24373979

AN - SCOPUS:84899621071

SN - 0927-7765

VL - 117

SP - 449

EP - 456

JO - Colloids and Surfaces B: Biointerfaces

JF - Colloids and Surfaces B: Biointerfaces

ER -

Surface modification and bioconjugation of FeCo magnetic nanoparticles with proteins

Abstract

Bibliographical note

Keywords

Access

OpenUrl availability

Other files and links

Fingerprint

Cite this