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Adsorption of human serum albumin in porous silicon gradients
Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology.
Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Applied Physics.
Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Applied Physics.
Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Applied Optics .ORCID iD: 0000-0001-9229-2028
2003 (English)Conference paper, Published paper (Other academic)
Abstract [en]

Backside etching has been utilized to produce gradients of pore size and layer thickness in porous silicon. Human serum albumin (HSA) was adsorbed on such gradients at two different pH values: 4.9, the pI of HSA, and 7.4, the physiological pH. The samples were investigated by scanning electron microscopy, spectroscopic ellipsometry, and autoradiography. The results show that the protein adsorbed displays a gradient along with the pore size and the thickness gradient. The higher than current density used during etching, the more sway-back shaped curves were seen for the protein adsorption pattern, independent of pH. When 50 mA/cm2 current density was used during etching, the quota between the maximal intensity value and the plateau value seen after adsorption of the HSA increased for pH 7.4.

Place, publisher, year, edition, pages
2003. Vol. 197, no 2, p. 326-330
National Category
Engineering and Technology
Identifiers
URN: urn:nbn:se:liu:diva-46654DOI: 10.1002/pssa.200306518OAI: oai:DiVA.org:liu-46654DiVA, id: diva2:267550
Available from: 2009-10-11 Created: 2009-10-11 Last updated: 2021-09-17
In thesis
1. Biomolecular Interactions with Porous Silicon
Open this publication in new window or tab >>Biomolecular Interactions with Porous Silicon
2003 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

One common problem when putting something inside the body is a fast response from the body defending it from the intruder. Here the researchers are struggling with finding biocompatible materials, which act in a predicted and non-harmful way. In the drug delivery area the idea is to find a good solution of giving a patient its daily medication in a convenient way. The ideal would be to have a unit that could deliver the drug automatically when needed in the dose needed. By high trough putscreening, finding of potential drugs or molecules related to diseases takes much less time. Here a large surface area to which the substance of interest can attach is preferable to be able to use as little analyte as possible and still have a high sensitivity.

To be able to realize the applications mentioned above a basic understanding of how proteins interact with surfaces must be developed.The aim of this thesis has been to investigate the adsorption of proteins into and on porous silicon.

Porous silicon was chosen as the porous material to work with because porous silicon has been shown to be bioactive and produce hydroxyapatite upon incubation in simulated body fluid. It is also a material with large surface area, which is convenient to use in the chiparea as well as in drug delivery.

Gradients in pore size and porous layer thickness were etched in silicon and used in protein adsorption experiments together with homogeneous porous layers. The adsorbed amounts of protein were determined at different pH, different protein concentrations as well as for porous silicon prepared with different etching conditions.

The results show that the morphology of the porous layer influence the protein uptake, indicating that more protein is found for larger pore sizes as well as for thicker porous layers. A minimum pore size of 5.5 nm in radius was found for albumin penetration. An increase in protein concentration up to 10 mg/ml albumin resulted in more proteins loaded into the porous silicon layer. The refractive index spectrum of carbonic anhydrase and location of the protein in porous silicon were also determined.

Place, publisher, year, edition, pages
Linköping: Linköping University, 2003. p. 117
Series
Linköping Studies in Science and Technology. Dissertations, ISSN 0345-7524 ; 804
National Category
Biophysics
Identifiers
urn:nbn:se:liu:diva-179304 (URN)9173736112 (ISBN)
Public defence
2003-04-11, Planck, Fysikhuset, Valla campus, Linköpings universitet, Linköping, 09:15
Opponent
Note

All or some of the partial works included in the dissertation are not registered in DIVA and therefore not linked in this post.

Available from: 2021-09-29 Created: 2021-09-17 Last updated: 2025-02-20Bibliographically approved

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Tengvall, PenttiLundström, IngemarArwin, Hans

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