Details
| Original language | English |
|---|---|
| Pages (from-to) | 51-57 |
| Number of pages | 7 |
| Journal | Microporous and Mesoporous Materials |
| Volume | 131 |
| Issue number | 1-3 |
| Publication status | Published - 2 Dec 2009 |
Abstract
The immobilization of a model enzyme, alkaline phosphatase (ALP), onto differently modified silica surfaces and coatings was investigated as a test case for the biofunctionalization of implant surfaces. In this context, the influence of silica surface structures and various silane linker molecules on the capacity to bind active proteins were studied. For this purpose, microscope glass slides were coated with unstructured or mesoporous silica films. The binding of the protein to the surface was mediated by trialkoxysilanes with different functional groups like amino, epoxy, and urea functions. The model protein ALP was chosen due to its robustness and the availability of a simple activity assay. This assay showed that all the functionalized trialkoxysilanes tested were able to immobilize active ALP on silica surfaces. Using the 3-aminopropylsilyl modification resulted in the highest activity of bound ALP, especially in combination with a mesoporous surface coating. Interestingly, unstructured silica sol-gel films had only low capacity to immobilize active enzyme whereas both mesoporous silica coatings and plain glass bound higher amounts of active ALP. By using mesoporous coatings functionalized with 3-aminopropylsilyl residues, maximal binding capacities for active ALP were achieved. This combination appears most promising for the further development of bioactive surfaces for practical applications such as surgical implant functionalization.
Keywords
- Alkaline phosphatase (ALP), Mesoporous coating, Protein immobilization, Silanization
ASJC Scopus subject areas
- Chemistry(all)
- Materials Science(all)
- Physics and Astronomy(all)
- Condensed Matter Physics
- Engineering(all)
- Mechanics of Materials
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In: Microporous and Mesoporous Materials, Vol. 131, No. 1-3, 02.12.2009, p. 51-57.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Immobilization of alkaline phosphatase on modified silica coatings
AU - Ehlert, Nina
AU - Müller, Peter Paul
AU - Stieve, Martin
AU - Behrens, Peter
PY - 2009/12/2
Y1 - 2009/12/2
N2 - The immobilization of a model enzyme, alkaline phosphatase (ALP), onto differently modified silica surfaces and coatings was investigated as a test case for the biofunctionalization of implant surfaces. In this context, the influence of silica surface structures and various silane linker molecules on the capacity to bind active proteins were studied. For this purpose, microscope glass slides were coated with unstructured or mesoporous silica films. The binding of the protein to the surface was mediated by trialkoxysilanes with different functional groups like amino, epoxy, and urea functions. The model protein ALP was chosen due to its robustness and the availability of a simple activity assay. This assay showed that all the functionalized trialkoxysilanes tested were able to immobilize active ALP on silica surfaces. Using the 3-aminopropylsilyl modification resulted in the highest activity of bound ALP, especially in combination with a mesoporous surface coating. Interestingly, unstructured silica sol-gel films had only low capacity to immobilize active enzyme whereas both mesoporous silica coatings and plain glass bound higher amounts of active ALP. By using mesoporous coatings functionalized with 3-aminopropylsilyl residues, maximal binding capacities for active ALP were achieved. This combination appears most promising for the further development of bioactive surfaces for practical applications such as surgical implant functionalization.
AB - The immobilization of a model enzyme, alkaline phosphatase (ALP), onto differently modified silica surfaces and coatings was investigated as a test case for the biofunctionalization of implant surfaces. In this context, the influence of silica surface structures and various silane linker molecules on the capacity to bind active proteins were studied. For this purpose, microscope glass slides were coated with unstructured or mesoporous silica films. The binding of the protein to the surface was mediated by trialkoxysilanes with different functional groups like amino, epoxy, and urea functions. The model protein ALP was chosen due to its robustness and the availability of a simple activity assay. This assay showed that all the functionalized trialkoxysilanes tested were able to immobilize active ALP on silica surfaces. Using the 3-aminopropylsilyl modification resulted in the highest activity of bound ALP, especially in combination with a mesoporous surface coating. Interestingly, unstructured silica sol-gel films had only low capacity to immobilize active enzyme whereas both mesoporous silica coatings and plain glass bound higher amounts of active ALP. By using mesoporous coatings functionalized with 3-aminopropylsilyl residues, maximal binding capacities for active ALP were achieved. This combination appears most promising for the further development of bioactive surfaces for practical applications such as surgical implant functionalization.
KW - Alkaline phosphatase (ALP)
KW - Mesoporous coating
KW - Protein immobilization
KW - Silanization
UR - http://www.scopus.com/inward/record.url?scp=77649238969&partnerID=8YFLogxK
U2 - 10.1016/j.micromeso.2009.11.040
DO - 10.1016/j.micromeso.2009.11.040
M3 - Article
AN - SCOPUS:77649238969
VL - 131
SP - 51
EP - 57
JO - Microporous and Mesoporous Materials
JF - Microporous and Mesoporous Materials
SN - 1387-1811
IS - 1-3
ER -