Evaluation of silica nanoparticle binding to major human blood proteins

• Published in: Nanoscale research letters 2014-12, Vol.9 (1), p.2493-2493, Article 668
• Main Authors: Hata, Katsutomo, Higashisaka, Kazuma, Nagano, Kazuya, Mukai, Yohei, Kamada, Haruhiko, Tsunoda, Shin-ichi, Yoshioka, Yasuo, Tsutsumi, Yasuo
• Format: Article
• Language: English
• Subjects: Chemistry and Materials Science; Materials Science; Molecular Medicine; Nano Express; Nanochemistry; Nanoscale Science and Technology; Nanotechnology; Nanotechnology and Microengineering
• ISSN: 1931-7573; 1556-276X; 1556-276X
• DOI: 10.1186/1556-276X-9-668

Nanomaterials are used for various biomedical applications because they are often more effective than conventional materials. Recently, however, it has become clear that the protein corona that forms on the surface of nanomaterials when they make contact with biological fluids, such as blood, influences the pharmacokinetics and biological responses induced by the nanomaterials. Therefore, when evaluating nanomaterial safety and efficacy, it is important to analyze the interaction between nanomaterials and proteins in biological fluids and to evaluate the effects of the protein corona. Here, we evaluated the interaction of silica nanoparticles, a commonly used nanomaterial, with the human blood proteins albumin, transferrin, fibrinogen, and IgG. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis showed that the amount of albumin, transferrin, and IgG binding to the silica particles increased as the particle size decreased under conditions where the silica particle mass remained the same. However, under conditions in which the specific surface area remained constant, there were no differences in the binding of human plasma proteins to the silica particles tested, suggesting that the binding of silica particles with human plasma proteins is dependent on the specific surface area of the silica particles. Furthermore, the amount of albumin, transferrin, and IgG binding to silica nanoparticles with a diameter of 70 nm (nSP70) and a functional amino group was lower than that with unmodified nSP70, although there was no difference in the binding between nSP70 with the surface modification of a carboxyl functional group and nSP70. These results suggest that the characteristics of nanomaterials are important for binding with human blood proteins; this information may contribute to the development of safe and effective nanomaterials.