Adsorption of bovine serum albumin on silicon dioxide nanoparticles: Impact of pH on nanoparticle-protein interactions

Brittany E. Givens; Nina D. Diklich; Jennifer Fiegel; Vicki H. Grassian

doi:10.1116/1.4982598

Adsorption of bovine serum albumin on silicon dioxide nanoparticles: Impact of pH on nanoparticle-protein interactions

Brittany E. Givens, Nina D. Diklich, Jennifer Fiegel, Vicki H. Grassian

Chemical and Materials Engineering

Research output: Contribution to journal › Article › peer-review

35 Scopus citations

Abstract

Bovine serum albumin (BSA) adsorbed on amorphous silicon dioxide (SiO₂) nanoparticles was studied as a function of pH across the range of 2 to 8. Aggregation, surface charge, surface coverage, and protein structure were investigated over this entire pH range. SiO₂ nanoparticle aggregation is found to depend upon pH and differs in the presence of adsorbed BSA. For SiO₂ nanoparticles truncated with hydroxyl groups, the largest aggregates were observed at pH 3, close to the isoelectric point of SiO₂ nanoparticles, whereas for SiO₂ nanoparticles with adsorbed BSA, the aggregate size was the greatest at pH 3.7, close to the isoelectric point of the BSA-SiO₂ complex. Surface coverage of BSA was also the greatest at the isoelectric point of the BSA-SiO₂ complex with a value of ca. 3 ±1 × 10¹¹ molecules cm^-2. Furthermore, the secondary protein structure was modified when compared to the solution phase at all pH values, but the most significant differences were seen at pH 7.4 and below. It is concluded that protein-nanoparticle interactions vary with solution pH, which may have implications for nanoparticles in different biological fluids (e.g., blood, stomach, and lungs).

Original language	English
Article number	02D404
Journal	Biointerphases
Volume	12
Issue number	2
DOIs	https://doi.org/10.1116/1.4982598
State	Published - Jun 1 2017

Bibliographical note

Funding Information:
Transmission electron microscopy was completed using the Central Microscopy Facility at the University of Iowa. Thermogravimetric analysis was done using the instrumentation in C. Allan Guymon laboratory at the University of Iowa in the Department of Chemical and Biochemical Engineering; assistance and training were provided by Jacob McLaughlin. This work was supported by the NSF CBET Award (NSF-1424502 and 1640936). Nina D. Diklich was supported by NSF REU Grant No. 1359063. Additional support for Brittany E. Givens was provided by the Alfred P. Sloan Foundation through the University of Iowa Center for Exemplary Mentoring. The authors also acknowledge helpful discussions with Zhenzhu Xu, Sarah C. Larsen, Imali A. Mudunkotuwa, and Sean E. Lehman.

ASJC Scopus subject areas

Chemistry (all)
Biomaterials
Materials Science (all)
Biochemistry, Genetics and Molecular Biology (all)
Physics and Astronomy (all)

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abstract = "Bovine serum albumin (BSA) adsorbed on amorphous silicon dioxide (SiO2) nanoparticles was studied as a function of pH across the range of 2 to 8. Aggregation, surface charge, surface coverage, and protein structure were investigated over this entire pH range. SiO2 nanoparticle aggregation is found to depend upon pH and differs in the presence of adsorbed BSA. For SiO2 nanoparticles truncated with hydroxyl groups, the largest aggregates were observed at pH 3, close to the isoelectric point of SiO2 nanoparticles, whereas for SiO2 nanoparticles with adsorbed BSA, the aggregate size was the greatest at pH 3.7, close to the isoelectric point of the BSA-SiO2 complex. Surface coverage of BSA was also the greatest at the isoelectric point of the BSA-SiO2 complex with a value of ca. 3 ±1 × 1011 molecules cm-2. Furthermore, the secondary protein structure was modified when compared to the solution phase at all pH values, but the most significant differences were seen at pH 7.4 and below. It is concluded that protein-nanoparticle interactions vary with solution pH, which may have implications for nanoparticles in different biological fluids (e.g., blood, stomach, and lungs).",

author = "Givens, {Brittany E.} and Diklich, {Nina D.} and Jennifer Fiegel and Grassian, {Vicki H.}",

note = "Funding Information: Transmission electron microscopy was completed using the Central Microscopy Facility at the University of Iowa. Thermogravimetric analysis was done using the instrumentation in C. Allan Guymon laboratory at the University of Iowa in the Department of Chemical and Biochemical Engineering; assistance and training were provided by Jacob McLaughlin. This work was supported by the NSF CBET Award (NSF-1424502 and 1640936). Nina D. Diklich was supported by NSF REU Grant No. 1359063. Additional support for Brittany E. Givens was provided by the Alfred P. Sloan Foundation through the University of Iowa Center for Exemplary Mentoring. The authors also acknowledge helpful discussions with Zhenzhu Xu, Sarah C. Larsen, Imali A. Mudunkotuwa, and Sean E. Lehman.",

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N1 - Funding Information: Transmission electron microscopy was completed using the Central Microscopy Facility at the University of Iowa. Thermogravimetric analysis was done using the instrumentation in C. Allan Guymon laboratory at the University of Iowa in the Department of Chemical and Biochemical Engineering; assistance and training were provided by Jacob McLaughlin. This work was supported by the NSF CBET Award (NSF-1424502 and 1640936). Nina D. Diklich was supported by NSF REU Grant No. 1359063. Additional support for Brittany E. Givens was provided by the Alfred P. Sloan Foundation through the University of Iowa Center for Exemplary Mentoring. The authors also acknowledge helpful discussions with Zhenzhu Xu, Sarah C. Larsen, Imali A. Mudunkotuwa, and Sean E. Lehman.

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N2 - Bovine serum albumin (BSA) adsorbed on amorphous silicon dioxide (SiO2) nanoparticles was studied as a function of pH across the range of 2 to 8. Aggregation, surface charge, surface coverage, and protein structure were investigated over this entire pH range. SiO2 nanoparticle aggregation is found to depend upon pH and differs in the presence of adsorbed BSA. For SiO2 nanoparticles truncated with hydroxyl groups, the largest aggregates were observed at pH 3, close to the isoelectric point of SiO2 nanoparticles, whereas for SiO2 nanoparticles with adsorbed BSA, the aggregate size was the greatest at pH 3.7, close to the isoelectric point of the BSA-SiO2 complex. Surface coverage of BSA was also the greatest at the isoelectric point of the BSA-SiO2 complex with a value of ca. 3 ±1 × 1011 molecules cm-2. Furthermore, the secondary protein structure was modified when compared to the solution phase at all pH values, but the most significant differences were seen at pH 7.4 and below. It is concluded that protein-nanoparticle interactions vary with solution pH, which may have implications for nanoparticles in different biological fluids (e.g., blood, stomach, and lungs).

AB - Bovine serum albumin (BSA) adsorbed on amorphous silicon dioxide (SiO2) nanoparticles was studied as a function of pH across the range of 2 to 8. Aggregation, surface charge, surface coverage, and protein structure were investigated over this entire pH range. SiO2 nanoparticle aggregation is found to depend upon pH and differs in the presence of adsorbed BSA. For SiO2 nanoparticles truncated with hydroxyl groups, the largest aggregates were observed at pH 3, close to the isoelectric point of SiO2 nanoparticles, whereas for SiO2 nanoparticles with adsorbed BSA, the aggregate size was the greatest at pH 3.7, close to the isoelectric point of the BSA-SiO2 complex. Surface coverage of BSA was also the greatest at the isoelectric point of the BSA-SiO2 complex with a value of ca. 3 ±1 × 1011 molecules cm-2. Furthermore, the secondary protein structure was modified when compared to the solution phase at all pH values, but the most significant differences were seen at pH 7.4 and below. It is concluded that protein-nanoparticle interactions vary with solution pH, which may have implications for nanoparticles in different biological fluids (e.g., blood, stomach, and lungs).

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Adsorption of bovine serum albumin on silicon dioxide nanoparticles: Impact of pH on nanoparticle-protein interactions

Abstract

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