Search: WFRF:(Rosengren Holmberg Jenny P)
> (2010-2014) >
Blood protein-polym...
Blood protein-polymer adsorption fingerprinting: Implications for understanding hemoocompatibility and for biomaterial design.
-
- Nilsson Ekdahl, Kristina (author)
- Linnéuniversitetet,Institutionen för naturvetenskap, NV
-
- Engberg, Anna E. (author)
- Linnéuniversitetet,Institutionen för naturvetenskap, NV
-
- Rosengren-Holmberg, Jenny P. (author)
- Linnéuniversitetet,Institutionen för naturvetenskap, NV
-
show more...
-
- Chen, H (author)
- University of Pennsylvania
-
- Lambris, JD (author)
- University of Pennsylvania
-
- Nicholls, Ian A. (author)
- Linnéuniversitetet,Institutionen för naturvetenskap, NV,BBCL
-
show less...
-
(creator_code:org_t)
- 2011-02-11
- 2011
- English.
-
In: Journal of Biomedical Materials Research. Part A. - : Wiley. - 1549-3296 .- 1552-4965. ; 97A:1, s. 74-84
- Related links:
-
https://europepmc.or...
-
show more...
-
https://urn.kb.se/re...
-
https://doi.org/10.1...
-
show less...
Abstract
Subject headings
Close
- The aim of this study was to create polymeric materials with known properties to study the preconditions for complement activation. Initially, 22 polymers were screened for complement activating capacity. Based on these results, six polymers (P1-P6) were characterized regarding physico-chemical parameters, for example, composition, surface area, pore size, and protein adsorption from human EDTA-plasma. P2, P4, and reference particles of polystyrene and polyvinyl chloride, were hydrophobic, bound low levels of protein and were poor complement activators. Their accessible surface was limited to protein adsorption in that they had pore diameters smaller than most plasma proteins. P1 and P3 were negatively charged and adsorbed IgG and C1q. A 10-fold difference in complement activation was attributed to the fact that P3 but not P1 bound high amounts of C1-inhibitor. The hydrophobic P5 and P6 were low complement activators. They selectively bound apolipoproteins Al and AIV (and vitronectin), which probably limited the binding of complement activators to the surface. We demonstrate the usefulness of the modus operandi to use a high-throughput procedure to synthesize a great number of novel substances, assay their physico-chemical properties with the aim to study the relationship between the initial protein coat on a surface and subsequent biological events. Data obtained from the six polymers characterized here, suggest that a complement-resistant surface should be hydrophobic, uncharged, and have a small available surface, accomplished by nanostructured topography. Additional attenuation of complement can be achieved by selective enrichment of inert proteins and inhibitors.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- Biochemistry
- Biokemi
- Biomedical Sciences
- Biomedicinsk vetenskap
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
To the university's database