Poly(L-lysine)-g-poly(ethylene glycol) layers on metal oxide surfaces:: Attachment mechanism and effects of polymer architecture on resistance to protein adsorption
Poly(L-lysine)-g-poly(ethylene glycol) layers on metal oxide surfaces:: Attachment mechanism and effects of polymer architecture on resistance to protein adsorption
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DOI：
10.1021/jp993359m
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发表时间：
2000-04-13
影响因子：
3.3
通讯作者：
Spencer, ND
中科院分区：
文献类型：
--
作者：
Kenausis, GL;Vörös, J;Spencer, ND
在医用植入物和生物亲和力传感器的血液接触材料的设计中，能够承受蛋白质吸附的表面和界面的产生是一个主要挑战。聚乙二醇基材料通常被认为是制备耐蛋白质材料的特别有效的候选材料。大多数金属生物材料都覆盖着一层保护性的、稳定的氧化膜；将这种已知与蛋白质强烈相互作用的氧化物表面转化为非相互作用的表面，需要对表面/界面结构进行特定的设计。用原位光波导光模谱和非原位X射线光电子能谱技术研究了一类基于聚(L-赖氨酸)-g-聚乙二醇(PLL-g-PEG)的共聚物在几种金属氧化物表面的自发吸附。由此产生的吸附层在减少血清和单个蛋白质(如纤维蛋白原)的吸附方面非常有效，众所周知，纤维蛋白原在导致生物材料表面诱导的血液凝固和血栓形成的一系列事件中发挥主要作用。吸附的蛋白质水平低至
The generation of surfaces and interfaces that are able to withstand protein adsorption is a major challenge in the design of blood-contacting materials for both medical implants and bioaffinity sensors. Poly(ethylene glycol)-derived materials are generally considered to be particularly effective candidates for the fabrication of protein-resistant materials. Most metallic biomaterials are covered by a protective, stable oxide film; converting such oxide surfaces, which are known to strongly interact with proteins, into noninteractive surfaces requires a specific design of the surface/interface architecture. A class of copolymers based on poly(L-lysine)g-poly(ethylene glycol) (PLL g-PEG) was found to spontaneously adsorb from aqueous solutions onto several metal oxide surfaces, such as TiO2, Si0.4Ti0.6O2 and Nb2O5, as measured by the in situ optical waveguide lightmode spectroscopy technique and by ex situ X-ray photoelectron spectroscopy. The resulting adsorbed layers are highly effective in reducing the adsorption both of blood serum and of individual proteins such as fibrinogen, which is known to play a major role in the cascade of events that lead to biomaterial-surface-induced blood coagulation and thrombosis. Adsorbed protein levels as low as