| 1. |
- Karlsson, L M, et al.
(författare)
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Adsorption of human serum albumin in porous silicon gradients
- 2003
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Ingår i: physica status solidi (a). - : Wiley. - 0031-8965 .- 1521-396X.
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Konferensbidrag (övrigt vetenskapligt/konstnärligt)abstract
- 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.
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| 2. |
- Karlsson, L M, et al.
(författare)
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Back-side etching A tool for making morphology gradients in porous silicon
- 2002
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Ingår i: Journal of the Electrochemical Society. - : The Electrochemical Society. - 0013-4651 .- 1945-7111. ; 149:12
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Tidskriftsartikel (refereegranskat)abstract
- A new method for preparing morphology gradients in electrochemically etched porous silicon layers in presented. The idea is to etch on the back side of the anode and thus utilize and inhomogenous electric field to control the pore size along a surface. The etching procedure resulted in a complex gradient in pore size, porosity, and porous layer thickness, which was studied by spectroscopic ellipsometry and scanning electron microscopy. The gradients are of interest, e.g., for biomaterials research, bio-sensor applications, and for basic studies of adsorption of organic molecules, like proteins. In order to investigate the potential of the gradient surfaces for protein adsorption studies, these were exposed to human serum albumin, and a gradient in the amount of adsorbed protein was observed.
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| 3. |
- Karlsson, L M, et al.
(författare)
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Penetration and loading of human serum albumin in porous silicon layers with different pore sizes and thicknesses
- 2003
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Ingår i: Journal of Colloid and Interface Science. - 0021-9797 .- 1095-7103. ; 266:1, s. 40-47
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Tidskriftsartikel (refereegranskat)abstract
- Human serum albumin was adsorbed into porous silicon layers with thickness up to 3 µm and with different mean pore radius in the range 4.5-10 nm. The adsorbed amount of protein was quantified by I125 radioactive labeling techniques and ellipsometry. The results show that albumin penetrated into the pores when the mean pore radius was larger than 5.5 nm, but could not totally occupy the available surface area when the layer thickness was larger than 1 µm. Loading of albumin both into porous layers and onto plane silicon as a function of albumin concentration was also investigated. These measurements show that loading of protein increased with protein concentration at least up to 10 mg/ml for porous silicon and up to 1 mg/ml for plane silicon. The maximum deposition into the type of porous layers used here was 28 µg/cm2, compared to 0.36 µg/cm2 for plane silicon. © 2003 Elsevier Inc. All rights reserved.
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| 4. |
- Sun, Xaoling, et al.
(författare)
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Peptide modified gold-coated polyurethanes as thrombin scavenging surfaces
- 2000
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Ingår i: Journal of Biomedical Materials Research. - 0021-9304 .- 1097-4636. ; 49:1, s. 66-78
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Tidskriftsartikel (refereegranskat)abstract
- Thin layers of gold were deposited on polyurethane film and chemisorbed with three peptides having an N-terminal cysteine: Cys-Pro-Arg, Cys-(L)Phe-Pro-Arg, and Cys-(D)Phe-Pro-Arg. The ability of these surfaces to act. as thrombin scavengers was evaluated. The peptides are related to the known thrombin inhibitor Phe-Pro-Arg chloromethyl ketone and were shown to have significant thrombin inhibitory activity in solution. Attachment of the peptides to gold was confirmed by water contact angle and X-ray photoelectron spectroscopy measurements. Thrombin adsorption from a buffer and plasma was investigated, and chromogenic substrate assays were carried out for thrombin activity on the surfaces and in the supernatant following adsorption. The data suggest that the peptide-modified surfaces are able to adsorb thrombin with high affinity from a buffer and that thrombin is taken up selectively from plasma. The Cys-(D)Phe-Pro-Arg modified surfaces showed particularly high affinity for thrombin. It was also found that the activity of thrombin adsorbed on the peptide surfaces was inhibited, and inhibition was greatest on the Cys(D)Phe-Pro-Arg surface. We concluded that the peptide surfaces may have potential as antithrombogenic materials via their ability to scavenge and inhibit thrombin generated as a result of blood-material contact.
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