Department of Physics, Chemistry and Biology, Linköping University, S-581 83 Linköping, Sweden.
Colloids Surf B Biointerfaces. 2010 Feb 1;75(2):410-7. doi: 10.1016/j.colsurfb.2009.09.013. Epub 2009 Oct 2.
Thick matrices of fibrinogen with incorporation of a matrix metalloproteinase inhibitor were covalently bonded on functionalized silicon surfaces using an ethyl-3-dimethyl-aminopropyl-carbodiimide and N-hydroxy-succinimide affinity ligand coupling chemistry. The growth of the structure was followed in situ using dynamic ellipsometry and characterized at steady-state with spectroscopic ellipsometry. The growth was compared with earlier work on ex situ growth of fibrinogen layers studied by single wavelength ellipsometry. It is found that in situ growth and ex situ growth yield different structural properties of the formed protein matrix. Fibrinogen matrices with thicknesses up to 58 nm and surface mass densities of 1.6 microg/cm2 have been produced.
使用乙基-3-二甲基氨基丙基碳化二亚胺和 N-羟基琥珀酰亚胺亲和配体偶联化学，将含有基质金属蛋白酶抑制剂的纤维蛋白原厚矩阵共价键合到功能化的硅表面上。使用动态椭圆测量法原位跟踪结构的生长，并通过光谱椭圆测量法在稳态下对其进行表征。将其与通过单波长椭圆测量法研究的纤维蛋白原层的体外生长的早期工作进行了比较。结果发现，原位生长和体外生长产生了不同的形成蛋白质基质的结构特性。已经生产出厚度高达 58nm 和表面质量密度为 1.6μg/cm2 的纤维蛋白原基质。
