Improving the design
of nanoparticles for use as drug carriers
or biosensors requires a better understanding of the protein–nanoparticle
interaction. Here, we present a new tool to investigate this interaction
in situ
and without additional labeling of the proteins
and/or nanoparticles. By combining nonresonant second-harmonic light
scattering with a modified Langmuir model, we show that it is possible
to gain insight into the adsorption behavior of blood proteins, namely
fibrinogen, human serum albumin, and transferrin, onto negatively
charged polystyrene nanoparticles. The modified Langmuir model gives
us access to the maximum amount of adsorbed protein, the apparent
binding constant, and Gibbs free energy. Furthermore, we employ the
method to investigate the influence of the nanoparticle size on the
adsorption of human serum albumin and find that the amount of adsorbed
protein increases more than the surface area per nanoparticle for
larger diameters.
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