Issue 22, 2015
From the journal:

Nanoscale

Low affinity binding of plasma proteins to lipid-coated quantum dots as observed by in situ fluorescence correlation spectroscopy†

Yvonne Klapper,a   Pauline Maffre,a   Li Shang,a   Kristina N. Ekdahl,bc   Bo Nilsson,c   Simon Hettler,d   Manuel Dries,d   Dagmar Gerthsend  and  G. Ulrich Nienhaus*aef  

* Corresponding authors

a Institute of Applied Physics and Center for Functional Nanostructures, Karlsruhe Institute of Technology (KIT), Karlsruhe, Germany
E-mail: uli@illinois.edu

b Linnæus Center of Biomaterials Chemistry, Linnæus University, Kalmar, Sweden

c Department of Immunology, Genetics and Pathology, Uppsala University, Uppsala, Sweden

d Laboratory of Electron Microscopy (LEM), KIT, Karlsruhe, Germany

e Institute of Toxicology and Genetics, KIT, Eggenstein-Leopoldshafen, Germany

f Department of Physics, University of Illinois at Urbana-Champaign, Illinois, USA

Abstract

Protein binding to lipid-coated nanoparticles has been pursued quantitatively by using fluorescence correlation spectroscopy. The binding of three important plasma proteins to lipid-enwrapped quantum dots (QDs) shows very low affinity, with an apparent dissociation coefficient in the range of several hundred micromolar. Thus, the tendency to adsorb is orders of magnitude weaker than for QDs coated with dihydrolipoic acid.

Graphical abstract: Low affinity binding of plasma proteins to lipid-coated quantum dots as observed by in situ fluorescence correlation spectroscopy

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Article information

DOI
https://doi.org/10.1039/C5NR01694K
Article type
Communication
Submitted
16 Mar 2015
Accepted
29 Apr 2015
First published
01 May 2015

Nanoscale, 2015,7, 9980-9984

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Low affinity binding of plasma proteins to lipid-coated quantum dots as observed by in situ fluorescence correlation spectroscopy

Y. Klapper, P. Maffre, L. Shang, K. N. Ekdahl, B. Nilsson, S. Hettler, M. Dries, D. Gerthsen and G. U. Nienhaus, Nanoscale, 2015, 7, 9980 DOI: 10.1039/C5NR01694K

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