Comparing protein adsorption onto alumina and silica nanomaterial surfaces: clues for vaccine adjuvant development
Protein adsorption onto nanomaterial surfaces is important for various nanobiotechnology applications such as biosensors and drug delivery. Within this scope, there is growing interest to develop alumina- and silica-based nanomaterial vaccine adjuvants and an outstanding need to compare protein adso...
| Main Authors: | , , , , |
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| Other Authors: | |
| Format: | Journal Article |
| Language: | English |
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2022
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| Online Access: | https://hdl.handle.net/10356/160545 |
| _version_ | 1811694022928891904 |
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| author | Park, Hyeonjin Ma, Gamaliel Junren Yoon, Bo Kyeong Cho, Nam-Joon Jackman, Joshua A. |
| author2 | School of Materials Science and Engineering |
| author_facet | School of Materials Science and Engineering Park, Hyeonjin Ma, Gamaliel Junren Yoon, Bo Kyeong Cho, Nam-Joon Jackman, Joshua A. |
| author_sort | Park, Hyeonjin |
| collection | NTU |
| description | Protein adsorption onto nanomaterial surfaces is important for various nanobiotechnology applications such as biosensors and drug delivery. Within this scope, there is growing interest to develop alumina- and silica-based nanomaterial vaccine adjuvants and an outstanding need to compare protein adsorption onto alumina- and silica-based nanomaterial surfaces. Herein, using alumina- and silica-coated arrays of silver nanodisks with plasmonic properties, we conducted localized surface plasmon resonance (LSPR) experiments to evaluate real-time adsorption of bovine serum albumin (BSA) protein onto alumina and silica surfaces. BSA monomers and oligomers were prepared in different water-ethanol mixtures and both adsorbing species consistently showed quicker adsorption kinetics and more extensive adsorption-related spreading on alumina surfaces as compared to on silica surfaces. We rationalized these experimental observations in terms of the electrostatic forces governing protein-surface interactions on the two nanomaterial surfaces and the results support that more rigidly attached BSA protein-based coatings can be formed on alumina-based nanomaterial surfaces. Collectively, the findings in this study provide fundamental insight into protein-surface interactions at nanomaterial interfaces and can help to guide the development of protein-based coatings for medical and biotechnology applications such as vaccines. |
| first_indexed | 2024-10-01T07:00:58Z |
| format | Journal Article |
| id | ntu-10356/160545 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T07:00:58Z |
| publishDate | 2022 |
| record_format | dspace |
| spelling | ntu-10356/1605452022-07-26T08:08:10Z Comparing protein adsorption onto alumina and silica nanomaterial surfaces: clues for vaccine adjuvant development Park, Hyeonjin Ma, Gamaliel Junren Yoon, Bo Kyeong Cho, Nam-Joon Jackman, Joshua A. School of Materials Science and Engineering Engineering::Materials Adsorption Protein Dynamics Protein adsorption onto nanomaterial surfaces is important for various nanobiotechnology applications such as biosensors and drug delivery. Within this scope, there is growing interest to develop alumina- and silica-based nanomaterial vaccine adjuvants and an outstanding need to compare protein adsorption onto alumina- and silica-based nanomaterial surfaces. Herein, using alumina- and silica-coated arrays of silver nanodisks with plasmonic properties, we conducted localized surface plasmon resonance (LSPR) experiments to evaluate real-time adsorption of bovine serum albumin (BSA) protein onto alumina and silica surfaces. BSA monomers and oligomers were prepared in different water-ethanol mixtures and both adsorbing species consistently showed quicker adsorption kinetics and more extensive adsorption-related spreading on alumina surfaces as compared to on silica surfaces. We rationalized these experimental observations in terms of the electrostatic forces governing protein-surface interactions on the two nanomaterial surfaces and the results support that more rigidly attached BSA protein-based coatings can be formed on alumina-based nanomaterial surfaces. Collectively, the findings in this study provide fundamental insight into protein-surface interactions at nanomaterial interfaces and can help to guide the development of protein-based coatings for medical and biotechnology applications such as vaccines. We acknowledge support from the Samsung Research Fund, Sungkyunkwan University, 2019. 2022-07-26T08:08:10Z 2022-07-26T08:08:10Z 2021 Journal Article Park, H., Ma, G. J., Yoon, B. K., Cho, N. & Jackman, J. A. (2021). Comparing protein adsorption onto alumina and silica nanomaterial surfaces: clues for vaccine adjuvant development. Langmuir, 37(3), 1306-1314. https://dx.doi.org/10.1021/acs.langmuir.0c03396 0743-7463 https://hdl.handle.net/10356/160545 10.1021/acs.langmuir.0c03396 33444030 2-s2.0-85099875172 3 37 1306 1314 en Langmuir © 2021 American Chemical Society. All rights reserved. |
| spellingShingle | Engineering::Materials Adsorption Protein Dynamics Park, Hyeonjin Ma, Gamaliel Junren Yoon, Bo Kyeong Cho, Nam-Joon Jackman, Joshua A. Comparing protein adsorption onto alumina and silica nanomaterial surfaces: clues for vaccine adjuvant development |
| title | Comparing protein adsorption onto alumina and silica nanomaterial surfaces: clues for vaccine adjuvant development |
| title_full | Comparing protein adsorption onto alumina and silica nanomaterial surfaces: clues for vaccine adjuvant development |
| title_fullStr | Comparing protein adsorption onto alumina and silica nanomaterial surfaces: clues for vaccine adjuvant development |
| title_full_unstemmed | Comparing protein adsorption onto alumina and silica nanomaterial surfaces: clues for vaccine adjuvant development |
| title_short | Comparing protein adsorption onto alumina and silica nanomaterial surfaces: clues for vaccine adjuvant development |
| title_sort | comparing protein adsorption onto alumina and silica nanomaterial surfaces clues for vaccine adjuvant development |
| topic | Engineering::Materials Adsorption Protein Dynamics |
| url | https://hdl.handle.net/10356/160545 |
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