Protein resistance of titanium oxide surfaces modified by biologically inspired mPEG-DOPA
Protein resistance of titanium oxide surfaces modified by biologically inspired mPEG-DOPA
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DOI：
10.1021/la048626g
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发表时间：
2005-01-18
期刊：
影响因子：
3.9
通讯作者：
Messersmith, PB
中科院分区：
文献类型：
--
作者：
Dalsin, JL;Lin, LJ;Messersmith, PB
在本研究中，我们利用X射线光电子能谱（XPS），光谱椭圆偏振（ELM），光波导光模光谱（OWLS）检查的表面吸附和蛋白质电阻行为的生物启发的聚合物组成的聚（乙二醇）（PEG）共轭肽模拟贻贝粘附蛋白。将贻贝粘附蛋白的关键组分3，4-二羟基苯丙氨酸（DOPA）的含有多达三个残基的肽缀合至单甲氧基封端的PEG聚合物。这些mPEG-DOPA聚合物被发现是高度粘附到二氧化钛表面，定量XPS分析提供了有用的洞察力的结合机制。此外，固定化PEG的抗氧化性反映在mPEG-DOPA改性的TiO 2表面对蛋白质吸附的优异抗性中。mPEG-DOPA和人血清吸附的测量结果与乙二醇（EG）表面密度和吸附的血清质量相关，并证明阈值约为15-20 EG/nm（2），高于该阈值时，蛋白质吸附量基本上很少。关于吸附的PEG的表面密度和吸附层的相关不结垢行为，在表面结合的mPEG-DOPA聚合物和使用其他方法固定到表面的PEG聚合物的不结垢性质之间存在强的相似性。含有三个多巴残基的肽锚导致PEG表面密度高于使用几种现有的PEG固定化策略所实现的那些，这表明贻贝粘附蛋白的肽模拟物可用于在表面上实现高密度的蛋白质抗性聚合物。
In the present study, we have utilized X-ray photoelectron spectroscopy (XPS), spectroscopic ellipsometry (ELM), and optical waveguide lightmode spectroscopy (OWLS) to examine the surface adsorption and protein resistance behavior of bio-inspired polymers consisting of poly(ethylene glycol) (PEG) conjugated to peptide mimics of mussel adhesive proteins. Peptides containing up to three residues of 3,4-dihydroxyphenylalanine (DOPA), a key component of mussel adhesive proteins, were conjugated to monomethoxy-terminated PEG polymers. These mPEG-DOPA polymers were found to be highly adhesive to TiO2 surfaces, with quantitative XPS analysis providing useful insight into the binding mechanism. Additionally, the antifouling properties of immobilized PEG were reflected in the excellent resistance of mPEG-DOPA-modified TiO2 surfaces to protein adsorption. Measurements of mPEG-DOPA and human serum adsorption were related in terms of ethylene glycol (EG) surface density and serum mass adsorbed and demonstrated a threshold of approximately 15-20 EG/nm(2), above which substantially little protein adsorbs. With respect to surface density of adsorbed PEG and the associated nonfouling behavior of the adlayers, strong parallels exist between the nonfouling properties of the surface-bound mPEG-DOPA polymers and PEG polymers immobilized to surfaces using other approaches. Peptide anchors containing three DOPA residues resulted in PEG surface densities higher than those achieved using several existing PEG immobilization strategies, suggesting that peptide mimics of mussel adhesive proteins may be useful for achieving high densities of protein-resistant polymers on surfaces.