Abstract
Context: Once inhaled, nanoparticles (NP) deposit on the lung surface and have first contact with the epithelial lung lining fluid (ELF) rich in proteins, which may bind to NP.
Objective: In this study, we investigate the parameters that influence the binding between NP and proteins.
Materials and methods: We used the proteins albumin, transferrin (TF), and apolipoprotein A-1 (all known as proteins from ELF) and different NP (polystyrene NP with negative, positive, and neutral surface coatings, Printex G and Printex 90) as models.
Results: In all cases, a linear correlation of the added NP amount and the amount of bound proteins was found and was described quantitatively by binding indices. Bovine serum albumin (BSA), TF, and apo A-1 were bound to the largest extent to hydrophobic NP, which shows the extraordinary importance of the NP’s surface properties.
Discussion: The binding index indicates the relevance of primary particle size and surface properties, including hydrophobicity.
Conclusion: Size and surface modifications of NP determine their protein binding. Our results suggest that the formation of conjugates of BSA, TF, and Apo A-1 with NP may play an important role in their translocation across the air–blood–barrier and subsequent biokinetics.
Acknowledgments
We are grateful for the technical assistance of Carola Eggert and Franz Erbe.
Declaration of interest
This work was partially supported by the US-National Institutes of Health, NIH grant HL074022, by the German Research Foundation (DFG) grants FOR627 and SPP1313, by EU FP6 project Particle-Risk contract No. 012912 (NEST), and by EU FP7 project NeuroNano, NMP4-SL-2008–214547.