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Adsorption of complement protein C3 at polymer surfaces and the demonstration of a specific binding of factor B by adsorbed C3
Institute for Surface Chemistry.
Institute for Surface Chemistry.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Biomedical Informatics and Engineering.
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1996 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 179, no 1, 163-172 p.Article in journal (Refereed) Published
Abstract [en]

The adsorption of C3 at poly(methyl methacrylate) (PMMA) and poly(styrene) (PS) surfaces was investigated within situellipsometry and compared to that at (hydrophilic and negatively charged) silica and (hydrophobic) methylated silica. The adsorption of C3 at PMMA was higher than that at PS, while the adsorbed layer thickness was the same for the two surfaces. For both PMMA and PS the adsorbed layer thickness (10 ± 2 nm) corresponds rather closely to that of end-on oriented C3 molecules. The adsorption of C3 at PMMA and PS was found to be intermediate between that at silica and methylated silica, although the adsorbed layer thickness was similar for all surfaces. The competitive adsorption among C3, human serum albumin (HSA), and factor B was investigated with ellipsometry and total internal reflection fluorescence spectroscopy (TIRF). Addition of HSA after C3 preadsorption resulted in fractional C3 desorption for both PMMA and PS. Factor B deposition at PS after preadsorption of C3 and blocking with HSA was found to be largely due to specific binding to C3/C3b, while in the case of PMMA, factor B was largely accumulated through passive (displacement) adsorption.

Place, publisher, year, edition, pages
1996. Vol. 179, no 1, 163-172 p.
National Category
Immunology in the medical area
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URN: urn:nbn:se:uu:diva-57419DOI: 10.1006/jcis.1996.0198OAI: oai:DiVA.org:uu-57419DiVA: diva2:85328
Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2017-12-04Bibliographically approved

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Westin, Jerker

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