| Autor: |
van Damme HS; Department of Chemical Technology, University of Twente, Enschede, The Netherlands., Beugeling T, Ratering MT, Feijen J |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of biomaterials science. Polymer edition [J Biomater Sci Polym Ed] 1991; Vol. 3 (1), pp. 69-84. |
| DOI: |
10.1163/156856292x00088 |
| Abstrakt: |
Protein adsorption of human serum albumin (HSA), human fibrinogen (Fg), human immunoglobulin G (IgG), high density lipoprotein (HDL) and high molecular weight kininogen (HMWK) from plasma onto poly (n-alkyl methacrylate) (PAMA) surfaces was measured using a semi-quantitative enzyme-immunoassay. Adsorption was investigated for PAMA(n = 1) (n is the number of C-atoms in the n-alkyl side chain), PAMA(n = 8) and PAMA(n = 18). PAMA(n = 1) has a relatively hydrophilic surface as compared to the more hydrophobic PAMA(n = 8) surface. Both polymers have surface chains which do not reorient after contact with water. The PAMA(n = 18) surface is relatively hydrophobic but in this case polymer surface chains and segments are able to reorient after contact with water. Protein adsorption was measured both as a function of time and as a function of the plasma dilution. If adsorption from plasma was measured as a function of time no exchange of proteins could be observed. The amount of adsorbed protein was always larger in the case of the hydrophobic PAMA(n = 8) as compared to PAMAS(n = 1 and 18), probably due to hydrophobic interactions between the proteins and the PAMA(n = 8) surface. At high plasma concentration relatively large amounts of HDL adsorb onto PAMA(n = 8), indicating that this lipoprotein preferentially adsorbs onto this surface. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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