Fibrinogen adsorption on blocked surface of albumin

Fibrinogen adsorption on blocked surface of albumin
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DOI:
10.1016/j.colsurfb.2010.12.016
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发表时间:
2011-05-01
影响因子:
5.8
通讯作者:
Hou, Xiaolin
Hou, Xiaolin
中科院分区:
工程技术2区
文献类型:
--
作者:
Holmberg, Maria;Hou, Xiaolin

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我们已经研究了白蛋白和纤维蛋白原的吸附到PET(聚对苯二甲酸乙二醇酯)和玻璃表面上,以及如何预吸附到这些表面上的白蛋白会影响后来添加的纤维蛋白原的吸附。对于暴露于血液的材料和器械,纤维蛋白原的吸附通常是不希望发生的事件,因为纤维蛋白原是凝血级联的一部分,并且纤维蛋白原的非特异性吸附可能对血小板的活化产生影响。白蛋白通常用作封闭剂,以避免非特异性蛋白质吸附到设计用于处理生物样品(包括蛋白质溶液)的装置的表面上。它是基于这样的假设,即蛋白质作为单层吸附在表面上,并且蛋白质不吸附在彼此之上。通过用发射具有不同能量的γ辐射的两种不同放射性碘同位素标记白蛋白和纤维蛋白原,在同一样品上同时监测白蛋白和纤维蛋白原的吸附。关于吸附的蛋白质层的形貌和覆盖的信息已经使用AFM(原子力显微镜)分析在液体中获得。我们的研究表明,白蛋白以多层方式吸附在PET上,当白蛋白预吸附在表面上时,纤维蛋白原吸附在白蛋白的顶部。(C)2010 Elsevier B.V.保留所有权利。
We have investigated the adsorption of albumin and fibrinogen onto PET (polyethylene terephthalate) and glass surfaces and how pre-adsorption of albumin onto these surfaces can affect the adsorption of later added fibrinogen. For materials and devices being exposed to blood, adsorption of fibrinogen is often a non-wanted event, since fibrinogen is part of the clotting cascade and unspecific adsorption of fibrinogen can have an influence on the activation of platelets. Albumin is often used as blocking agent for avoiding unspecific protein adsorption onto surfaces in devices designed to handle biological samples, including protein solutions. It is based on the assumption that proteins adsorbs as a monolayer on surfaces and that proteins do not adsorb on top of each other. By labelling albumin and fibrinogen with two different radioactive iodine isotopes that emit gamma radiation with different energies, the adsorption of both albumin and fibrinogen has been monitored simultaneously on the same sample. Information about topography and coverage of adsorbed protein layers has been obtained using AFM (Atomic Force Microscopy) analysis in liquid. Our studies show that albumin adsorbs in a multilayer fashion on PET and that fibrinogen adsorbs on top of albumin when albumin is pre-adsorbed on the surfaces. (C) 2010 Elsevier B.V. All rights reserved.