Formation and cross-linking of fibrinogen layers monitored with in situ spectroscopic ellipsometry

• 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.

Ämnesord

MEDICIN OCH HÄLSOVETENSKAP  -- Klinisk medicin -- Odontologi (hsv//swe)

MEDICAL AND HEALTH SCIENCES  -- Clinical Medicine -- Dentistry (hsv//eng)

Nyckelord

Fibrinogen

ellipsometry

coupling chemistry

protein adsorption

NATURAL SCIENCES

NATURVETENSKAP

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vet (ämneskategori)

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