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Issue 9, 2013
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Cellular binding of anionic nanoparticles is inhibited by serum proteins independent of nanoparticle composition

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Abstract

Nanoparticles used in biological applications encounter a complex mixture of extracellular proteins. Adsorption of these proteins on the nanoparticle surface results in the formation of a “protein corona,” which can dominate the interaction of the nanoparticle with the cellular environment. The goal of this research was to determine how nanoparticle composition and surface modification affect the cellular binding of protein-nanoparticle complexes. We examined the cellular binding of a collection of commonly used anionic nanoparticles: quantum dots, colloidal gold nanoparticles, and low-density lipoprotein particles, in the presence and absence of extracellular proteins. These experiments have the advantage of comparing different nanoparticles under identical conditions. Using a combination of fluorescence and dark field microscopy, flow cytometry, and spectroscopy, we find that cellular binding of these anionic nanoparticles is inhibited by serum proteins independent of nanoparticle composition or surface modification. We expect these results will aid in the design of nanoparticles for in vivo applications.

Graphical abstract: Cellular binding of anionic nanoparticles is inhibited by serum proteins independent of nanoparticle composition

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Publication details

The article was received on 10 May 2013, accepted on 06 Jun 2013 and first published on 20 Jun 2013


Article type: Paper
DOI: 10.1039/C3BM60121H
Citation: Biomater. Sci., 2013,1, 975-982
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    Cellular binding of anionic nanoparticles is inhibited by serum proteins independent of nanoparticle composition

    C. C. Fleischer, U. Kumar and C. K. Payne, Biomater. Sci., 2013, 1, 975
    DOI: 10.1039/C3BM60121H

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