Effect of Bovine Serum Albumin Treatment on the Aging and Activity of Antibodies in Paper Diagnostics
Paper and cellulosic films are used in many designs of low-cost diagnostics such as paper-based blood grouping devices. A major issue limiting their commercialization is the short stability of the functional biomolecules. To address this problem, the effect of relative humidity (RH) and bovine serum...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2018-05-01
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| Series: | Frontiers in Chemistry |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/article/10.3389/fchem.2018.00161/full |
| _version_ | 1818542136459526144 |
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| author | Ziwei Huang Thomas Gengenbach Junfei Tian Wei Shen Gil Garnier |
| author_facet | Ziwei Huang Thomas Gengenbach Junfei Tian Wei Shen Gil Garnier |
| author_sort | Ziwei Huang |
| collection | DOAJ |
| description | Paper and cellulosic films are used in many designs of low-cost diagnostics such as paper-based blood grouping devices. A major issue limiting their commercialization is the short stability of the functional biomolecules. To address this problem, the effect of relative humidity (RH) and bovine serum albumin (BSA) on the antibody bioactivity and the surface chemical composition of a paper blood typing biodiagnostic were studied. An IgM blood typing antibody was physisorbed from solution onto paper - with or without BSA pretreatment, and aged for periods up to 9 weeks under various conditions with a series of RH. The blood typing efficiency of the antibodies and the substrate surface chemical composition were analyzed by image analysis and X-ray photoelectron spectroscopy (XPS), respectively. This study tests two hypotheses. The first is that the hydroxyl groups in paper promote antibody denaturation on paper; the second hypothesis is that proteins such as BSA can partially block the hydroxyl groups within paper, thus preserving antibody bioactivity. Results show that high RH is detrimental to antibody longevity on paper, while BSA can block hydroxyl groups and prolong antibody longevity by almost an order of magnitude—regardless of humidity. This study opens up new engineering concepts to develop robust and marketable paper diagnostics. The simplest is to store paper and antibody based diagnostics in moisture proof packages. |
| first_indexed | 2024-12-11T22:18:11Z |
| format | Article |
| id | doaj.art-b711fca591234e8a90707913a39ef2f0 |
| institution | Directory Open Access Journal |
| issn | 2296-2646 |
| language | English |
| last_indexed | 2024-12-11T22:18:11Z |
| publishDate | 2018-05-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Chemistry |
| spelling | doaj.art-b711fca591234e8a90707913a39ef2f02022-12-22T00:48:32ZengFrontiers Media S.A.Frontiers in Chemistry2296-26462018-05-01610.3389/fchem.2018.00161342794Effect of Bovine Serum Albumin Treatment on the Aging and Activity of Antibodies in Paper DiagnosticsZiwei Huang0Thomas Gengenbach1Junfei Tian2Wei Shen3Gil Garnier4BioPRIA, Department of Chemical Engineering, Monash University, Clayton, MO, AustraliaCSIRO Manufacturing, Clayton, MO, AustraliaBioPRIA, Department of Chemical Engineering, Monash University, Clayton, MO, AustraliaBioPRIA, Department of Chemical Engineering, Monash University, Clayton, MO, AustraliaBioPRIA, Department of Chemical Engineering, Monash University, Clayton, MO, AustraliaPaper and cellulosic films are used in many designs of low-cost diagnostics such as paper-based blood grouping devices. A major issue limiting their commercialization is the short stability of the functional biomolecules. To address this problem, the effect of relative humidity (RH) and bovine serum albumin (BSA) on the antibody bioactivity and the surface chemical composition of a paper blood typing biodiagnostic were studied. An IgM blood typing antibody was physisorbed from solution onto paper - with or without BSA pretreatment, and aged for periods up to 9 weeks under various conditions with a series of RH. The blood typing efficiency of the antibodies and the substrate surface chemical composition were analyzed by image analysis and X-ray photoelectron spectroscopy (XPS), respectively. This study tests two hypotheses. The first is that the hydroxyl groups in paper promote antibody denaturation on paper; the second hypothesis is that proteins such as BSA can partially block the hydroxyl groups within paper, thus preserving antibody bioactivity. Results show that high RH is detrimental to antibody longevity on paper, while BSA can block hydroxyl groups and prolong antibody longevity by almost an order of magnitude—regardless of humidity. This study opens up new engineering concepts to develop robust and marketable paper diagnostics. The simplest is to store paper and antibody based diagnostics in moisture proof packages.http://journal.frontiersin.org/article/10.3389/fchem.2018.00161/fullantibody bioactivityBSApaper diagnosticprotein stabilityantibody adsorption |
| spellingShingle | Ziwei Huang Thomas Gengenbach Junfei Tian Wei Shen Gil Garnier Effect of Bovine Serum Albumin Treatment on the Aging and Activity of Antibodies in Paper Diagnostics Frontiers in Chemistry antibody bioactivity BSA paper diagnostic protein stability antibody adsorption |
| title | Effect of Bovine Serum Albumin Treatment on the Aging and Activity of Antibodies in Paper Diagnostics |
| title_full | Effect of Bovine Serum Albumin Treatment on the Aging and Activity of Antibodies in Paper Diagnostics |
| title_fullStr | Effect of Bovine Serum Albumin Treatment on the Aging and Activity of Antibodies in Paper Diagnostics |
| title_full_unstemmed | Effect of Bovine Serum Albumin Treatment on the Aging and Activity of Antibodies in Paper Diagnostics |
| title_short | Effect of Bovine Serum Albumin Treatment on the Aging and Activity of Antibodies in Paper Diagnostics |
| title_sort | effect of bovine serum albumin treatment on the aging and activity of antibodies in paper diagnostics |
| topic | antibody bioactivity BSA paper diagnostic protein stability antibody adsorption |
| url | http://journal.frontiersin.org/article/10.3389/fchem.2018.00161/full |
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