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

被引：17

作者：

Berlind, T. ^{[1
]}

Poksinski, M. ^{[2
]}

Tengvall, P. ^{[1
]}

Arwin, H. ^{[1
]}

机构：

[1] Linkoping Univ, Dept Phys Chem & Biol, S-58183 Linkoping, Sweden

[2] Roxen IS AB, S-58105 Linkoping, Sweden

来源：

COLLOIDS AND SURFACES B-BIOINTERFACES | 2010年 / 75卷 / 02期

关键词：

Fibrinogen; Ellipsometry; Coupling chemistry; Protein adsorption; PROTEIN LAYERS; ADSORPTION; SURFACES; SILICON; CHEMISTRY; ALBUMIN;

D O I：

10.1016/j.colsurfb.2009.09.013

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

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 mu g/cm(2) have been produced. (C) 2009 Elsevier B.V. All rights reserved.

引用

页码：410 / 417

页数：8

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