Open AccessIn Situ Label-Free Study of Protein Adsorption on Nanoparticles
Author(s) -
Christoph Bernhard,
MarcJan van Zadel,
Alexander Bunn,
Mischa Bonn,
Grazia Gonella
Publication year - 2021
Publication title -
the journal of physical chemistry. b
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.864
H-Index - 392
eISSN - 1520-6106
pISSN - 1520-5207
DOI - 10.1021/acs.jpcb.1c04775
Subject(s) - adsorption , nanoparticle , protein adsorption , chemistry , langmuir adsorption model , in situ , human serum albumin , biosensor , biophysics , gelatin , bovine serum albumin , nanotechnology , chemical engineering , materials science , chromatography , biochemistry , organic chemistry , engineering , biology
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.