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Evaluation of silica nanoparticle binding to major human blood proteins.

Hata K, Higashisaka K, Nagano K, Mukai Y, Kamada H, Tsunoda S, Yoshioka Y, Tsutsumi Y - Nanoscale Res Lett (2014)

Bottom Line: Nanomaterials are used for various biomedical applications because they are often more effective than conventional materials.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.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.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Toxicology and Safety Science, Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamadaoka, Suita, Osaka, 565-0871, Japan, k-hata@towayakuhin.co.jp.

ABSTRACT
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.

No MeSH data available.


Effects of the specific surface area of silica particles on binding to human plasma proteins. Each protein solution was mixed with SP70, nSP100, nSP300, or mSP1000 at 1.75, 2.5, 7.41, and 25 mg/mL, respectively (i.e., approximately 1.5 × 104 mm2 of specific surface area). After centrifugation, each sample was separated by SDS-PAGE. The gel was stained by CBB staining, and the protein bands of albumin (A), transferrin (B), IgG (C), and fibrinogen (D) were quantified with the ImageJ software. The protein content of each band was estimated from its optical density compared with the optical density of each standard solution. Data are presented as the mean ± SD; n = 3; **P < 0.01 vs. nSP70-treated group; *P < 0.05 vs. nSP70-treated group; N.D., not detected.
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Fig2: Effects of the specific surface area of silica particles on binding to human plasma proteins. Each protein solution was mixed with SP70, nSP100, nSP300, or mSP1000 at 1.75, 2.5, 7.41, and 25 mg/mL, respectively (i.e., approximately 1.5 × 104 mm2 of specific surface area). After centrifugation, each sample was separated by SDS-PAGE. The gel was stained by CBB staining, and the protein bands of albumin (A), transferrin (B), IgG (C), and fibrinogen (D) were quantified with the ImageJ software. The protein content of each band was estimated from its optical density compared with the optical density of each standard solution. Data are presented as the mean ± SD; n = 3; **P < 0.01 vs. nSP70-treated group; *P < 0.05 vs. nSP70-treated group; N.D., not detected.

Mentions: We also evaluated the effect of the specific surface area of the silica particles on binding to human plasma proteins. The specific surface areas of each particle were matched with that of 25 mg/mL of mSP1000 (about 1.5 × 104 mm2), because mSP1000 was the largest particle in this study. The results showed that there was no significant difference in binding with each protein among each size of silica particle tested (Figure 2A,B,C,D), suggesting that the binding of silica particles to human plasma proteins is dependent on the specific surface area of the silica particles.Figure 2


Evaluation of silica nanoparticle binding to major human blood proteins.

Hata K, Higashisaka K, Nagano K, Mukai Y, Kamada H, Tsunoda S, Yoshioka Y, Tsutsumi Y - Nanoscale Res Lett (2014)

Effects of the specific surface area of silica particles on binding to human plasma proteins. Each protein solution was mixed with SP70, nSP100, nSP300, or mSP1000 at 1.75, 2.5, 7.41, and 25 mg/mL, respectively (i.e., approximately 1.5 × 104 mm2 of specific surface area). After centrifugation, each sample was separated by SDS-PAGE. The gel was stained by CBB staining, and the protein bands of albumin (A), transferrin (B), IgG (C), and fibrinogen (D) were quantified with the ImageJ software. The protein content of each band was estimated from its optical density compared with the optical density of each standard solution. Data are presented as the mean ± SD; n = 3; **P < 0.01 vs. nSP70-treated group; *P < 0.05 vs. nSP70-treated group; N.D., not detected.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4493834&req=5

Fig2: Effects of the specific surface area of silica particles on binding to human plasma proteins. Each protein solution was mixed with SP70, nSP100, nSP300, or mSP1000 at 1.75, 2.5, 7.41, and 25 mg/mL, respectively (i.e., approximately 1.5 × 104 mm2 of specific surface area). After centrifugation, each sample was separated by SDS-PAGE. The gel was stained by CBB staining, and the protein bands of albumin (A), transferrin (B), IgG (C), and fibrinogen (D) were quantified with the ImageJ software. The protein content of each band was estimated from its optical density compared with the optical density of each standard solution. Data are presented as the mean ± SD; n = 3; **P < 0.01 vs. nSP70-treated group; *P < 0.05 vs. nSP70-treated group; N.D., not detected.
Mentions: We also evaluated the effect of the specific surface area of the silica particles on binding to human plasma proteins. The specific surface areas of each particle were matched with that of 25 mg/mL of mSP1000 (about 1.5 × 104 mm2), because mSP1000 was the largest particle in this study. The results showed that there was no significant difference in binding with each protein among each size of silica particle tested (Figure 2A,B,C,D), suggesting that the binding of silica particles to human plasma proteins is dependent on the specific surface area of the silica particles.Figure 2

Bottom Line: Nanomaterials are used for various biomedical applications because they are often more effective than conventional materials.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.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.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Toxicology and Safety Science, Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamadaoka, Suita, Osaka, 565-0871, Japan, k-hata@towayakuhin.co.jp.

ABSTRACT
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.

No MeSH data available.