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Profiling of nanoparticle–protein interactions by electrophoresis techniques

  • Mohammad Zarei
  • Jamal Aalaie
Review
  • 1 Downloads

Abstract

The use of nanomaterials in the chemical, biomedical, and biotechnological sciences is growing, increasing the possible release of these materials into the environment and contact with living organisms. Because of their large surface area, biomolecules can be adsorbed on the surface of nanomaterials. Proteins bind to the surface of nanoparticles (NPs), forming a biological layer around the NP, the “protein corona,” which gives new characteristics to the NPs in biological milieu and may affect biomedical applications or induce nanotoxicological effects. Therefore, the development of analytical tools for identification of NP protein corona behavior is essential. Techniques such as spectroscopy, chromatography, calorimetry, and electrophoresis have been used to investigate the interaction of NPs with proteins. This review describes recent developments in the application of electrophoresis techniques for profiling of NP–protein interactions. Further, we provide an overview of directions and challenges in the application of electrophoresis methods for the investigation of NP–protein structures.

Graphical abstract

Keywords

Separation Electrophoresis Mass spectrometry Protein corona Nanoparticle 

Abbreviations

C3

Complement component 3

CD

Circular dichroism

CE

Capillary electrophoresis

DIGE

Difference gel electrophoresis

ICP

Inductively coupled plasma

ITC

Isothermal titration calorimetry

LC

Liquid chromatography

MS

Mass spectrometry

MS/MS

Tandem mass spectrometry

NMR

Nuclear magnetic resonance

NP

Nanoparticle

PDADMAC

Poly(diallyldimethylammonium chloride)

PAGE

Polyacrylamide gel electrophoresis

PSS

Poly(sodium 4-styrenesulfonate)

SDS

Sodium dodecyl sulfate

SILAC

Stable isotope labeling by amino acids in cell culture

SPIO

Superparamagnetic iron oxide

SPR

Surface plasmon resonance

Notes

Compliance with ethical standards

Conflict of interest

The authors declare that they have no competing interests

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Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Chemical, Polymer & Petrochemical Technology Development Research DivisionResearch Institute of Petroleum IndustryTehranIran

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