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The Relation Between Protein Adsorption and Hemocompatibility of Antifouling Polymer Brushes
Z. Riedelová, A. de Los Santos Pereira, J. Svoboda, O. Pop-Georgievski, P. Májek, K. Pečánková, F. Dyčka, C. Rodriguez-Emmenegger, T. Riedel
Language English Country Germany
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Adsorption MeSH
- Biocompatible Materials pharmacology chemistry MeSH
- Biofouling * prevention & control MeSH
- Humans MeSH
- Polymers chemistry MeSH
- Surface Properties MeSH
- Proteins MeSH
- Thrombosis * MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
Whenever an artificial surface comes into contact with blood, proteins are rapidly adsorbed onto its surface. This phenomenon, termed fouling, is then followed by a series of undesired reactions involving activation of complement or the coagulation cascade and adhesion of leukocytes and platelets leading to thrombus formation. Thus, considerable efforts are directed towards the preparation of fouling-resistant surfaces with the best possible hemocompatibility. Herein, a comprehensive hemocompatibility study after heparinized blood contact with seven polymer brushes prepared by surface-initiated atom transfer radical polymerization is reported. The resistance to fouling is quantified and thrombus formation and deposition of blood cellular components on the coatings are analyzed. Moreover, identification of the remaining adsorbed proteins is performed via mass spectroscopy to elucidate their influence on the surface hemocompatibility. Compared with an unmodified glass surface, the grafting of polymer brushes minimizes the adhesion of platelets and leukocytes and prevents the thrombus formation. The fouling from undiluted blood plasma is reduced by up to 99%. Most of the identified proteins are connected with the initial events of foreign body reaction towards biomaterial (coagulation cascade proteins, complement component, and inflammatory proteins). In addition, several proteins that are not previously linked with blood-biomaterial interaction are presented and discussed.
DWI Leibniz Institute for Interactive Materials Forckenbeckstraße 50 D 52074 Aachen Germany
Institució Catalana de Recerca i Estudis Avançats Passeig Lluís Companys 23 Barcelona 08010 Spain
Institute for Bioengineering of Catalonia Carrer de Baldiri Reixac 10 12 Barcelona 08028 Spain
Institute of Hematology and Blood Transfusion U Nemocnice 1 Prague 128 00 Czech Republic
References provided by Crossref.org
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