Atomic force microscope studies of fibrinogen adsorption

被引：19

作者：

Averett, Laurel E. ^{[2
]}

Schoenfisch, Mark H. ^{[1
]}

机构：

[1] Univ N Carolina, Dept Chem, Chapel Hill, NC 27599 USA

[2] Univ N Carolina, Dept Phys, Chapel Hill, NC 27599 USA

来源：

ANALYST | 2010年 / 135卷 / 06期

基金：

美国国家科学基金会;

关键词：

HUMAN PLASMA-FIBRINOGEN; ORIENTED PYROLYTIC-GRAPHITE; COMPONENT PROTEIN FILMS; 316L STAINLESS-STEEL; ADSORBED FIBRINOGEN; CONFORMATIONAL-CHANGES; SURFACE WETTABILITY; AQUEOUS CONDITIONS; PROBE MICROSCOPY; POLYMER SURFACES;

D O I：

10.1039/b924814e

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

Since its invention in 1986 by Binnig, Quate, and Gerber, the atomic force microscope (AFM) has proven to be an extremely useful tool for examining the interactions of proteins with surfaces. Fibrinogen in particular has been used as a model protein to demonstrate new methodologies for studying protein behavior with AFM due to its unique size, shape, and function. Indeed, fibrinogen's central role in both blood coagulation and blood-based infections has made it the primary protein used to interrogate the biocompatibility of surfaces. The goal of this review is to provide an analytical perspective on the utility of AFM for investigating the interaction of fibrinogen with surfaces.

引用

页码：1201 / 1209

页数：9

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