Formation and cross-linking of fibrinogen layers monitored with in situ spectroscopic ellipsometry
2010 (English)In: Colloids and Surfaces B: Biointerfaces, ISSN 0927-7765, E-ISSN 1873-4367, Vol. 75, no 2, 410-417 p.Article in journal (Other academic) Published
Thick matrices of fibrinogen with incorporation of a matrix metalloproteinaseinhibitor were covalently bonded on functionalized silicon surfaces using an ethyl-3-dimethyl-aminopropyl-carbodiimide and N-hydroxy-succinimide affinity ligand couplingchemistry. The growth of the structure was followed in situ using dynamic ellipsometryand characterized at steady-state with spectroscopic ellipsometry. The growth wascompared with earlier work on ex situ growth of fibrinogen layers studied by singlewavelength ellipsometry. It is found that in situ growth and ex situ growth yield differentstructural properties of the formed protein matrix. Fibrinogen matrices with thicknessesup to 58 nm and surface mass densities of 1.6 μg/cm2 have been produced.
Place, publisher, year, edition, pages
2010. Vol. 75, no 2, 410-417 p.
Fibrinogen, ellipsometry, coupling chemistry, protein adsorption
IdentifiersURN: urn:nbn:se:liu:diva-19707DOI: 10.1016/j.colsurfb.2009.09.013ISI: 000276921900004OAI: oai:DiVA.org:liu-19707DiVA: diva2:227667
Torun Berlind, Michal Poksinski, Pentti Tengvall and Hans Arwin, Formation and cross-linking of fibrinogen layers monitored with in situ spectroscopic ellipsometry, Colloids and Surfaces B: Biointerfaces, 2010, (75), 2, 410-417.
Copyright: Elsevier Science B.V., Amsterdam.