Characterization of protein adsorption onto FePt nanoparticles using dual-focus fluorescence correlation spectroscopy

• Pauline Maffre,
• Karin Nienhaus,
• Faheem Amin,
• Wolfgang J. Parak and
• G. Ulrich Nienhaus

Beilstein J. Nanotechnol. 2011, 2, 374–383, doi:10.3762/bjnano.2.43

• understand the structural and dynamic properties of the protein corona at the molecular level. Recently, we have used quantitative fluorescence microscopy, especially fluorescence correlation spectroscopy (FCS), to study protein adsorption of human serum albumin (HSA) on polymer-coated FePt NPs with an

• overall diameter of 11 nm [11]. HSA is the major soluble constituent of human blood plasma. It serves primarily as a carrier protein for steroids, fatty acids, and thyroid hormones [18]. We found that, at concentrations typically found in blood serum, ~20 HSA molecules adsorb as a monolayer of ~3.3 nm

• equilibrium binding of three abundant blood plasma proteins to FePt NPs, HSA (which was included to ensure that our previously reported data [11] can be reproduced with our new technique) and the apolipoproteins apoA-I and apoE4. These two proteins function as transporters for lipid molecules in the blood by