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Adsorbed Polyzwitterion Copolymer Layers Designed for Protein Repellency and Interfacial Retention
Langmuir ( IF 3.7 ) Pub Date : 2017-11-14 00:00:00 , DOI: 10.1021/acs.langmuir.7b03391
S. Kalasin 1 , R. A. Letteri 1 , T. Emrick 1 , M. M. Santore 1
Affiliation  

Poly(2-methacryloyloxyethyl phosphorylcholine) (pMPC), when end-tethered to surfaces by the adsorption of copolymeric cationic segments, forms adsorbed layers that substantially reduce protein adsorption. This study examined variations in the molecular architecture of copolymers containing cationic poly(trimethylammonium ethyl methacrylate (pTMAEMA) anchor blocks that adsorbed strongly to negative surfaces. With appropriate copolymer design, the pTMAEMA blocks were shielded, by pMPC tethers, from solution-phase proteins. The most protein-resistant copolymer layers, eliminating fibrinogen and lysozyme adsorption within detectible limits of 0.01 mg/m2, had metrics (the amount of pMPC at the surface and the reduced tether footprint) consistent with the formation of an interfacial polymer brush. The p(TMAEMA-b-MPC) copolymer layers substantially outperformed the protein resistance of surface-polymerized pMPC layers when compared on a per-polyzwitterion-mass basis or on the basis of the scaled tether area. Additionally, p(TMAEMA-b-MPC) copolymer layers offered advantages over the much-studied cationically anchored poly(ethylene glycol) (PEG) graft copolymer system, which forms PEG brushes by the adsorption of a poly l-lysine (PLL) backbone. Although the optimized p(TMAEMA-b-MPC) and PLL-PEG copolymers were similarly fibrinogen-resistant, the cationic protein lysozyme was repelled by pMPC but adhered to the PEG brush via PEG–lysozyme attractions. Additionally, the adsorbed p(TMAEMA-b-MPC) copolymers were not displaced by poly l-lysine homopolymers, which completely displaced the PLL-PEG copolymer to expose a protein-adhesive surface. Thus, the p(TMAEMA-b-MPC) copolymer system comprises a scalable means to produce protein-repellent surfaces, free of the complexities of surface-initiated polymerization and with the advantages of polyzwitterions.

中文翻译:

专为蛋白质排斥和界面保留设计的吸附式两性离子共聚物层

当聚(2-甲基丙烯酰氧基乙基磷酰胆碱)(pMPC)通过共聚阳离子链段的吸附而末端束缚在表面上时,形成的吸附层会大大降低蛋白质的吸附。这项研究研究了含有阳离子聚甲基丙烯酸三甲基铵乙酯(pTMAEMA)锚固嵌段的共聚物分子结构的变化,该锚固嵌段强烈吸附在负极表面上,通过适当的共聚物设计,pTMAEMA嵌段被pMPC束缚物从溶液相蛋白中屏蔽了。具有最强蛋白质抵抗力的共聚物层,在0.01 mg / m 2的可检测限内消除了纤维蛋白原和溶菌酶的吸附,其度量标准(表面上的pMPC量和减少的系链足迹)与界面聚合物刷的形成一致。 p(TMAEMA-当以每两性离子质量为基础或以缩放的系链面积为基础进行比较时,b- MPC)共聚物层基本上优于表面聚合的pMPC层的蛋白质抗性。此外,p(TMAEMA- b -MPC)共聚物层比经过广泛研究的阳离子锚定聚乙二醇(PEG)接枝共聚物系统具有优势,后者通过吸附聚l-赖氨酸(PLL)主链形成PEG刷。尽管优化的p(TMAEMA- b -MPC)和PLL-PEG共聚物对纤维蛋白原具有类似的抗性,但阳离子蛋白溶菌酶却被pMPC排斥,但通过PEG-溶菌酶吸引力附着在PEG刷上。另外,吸附的p(TMAEMA- b -MPC)共聚物不会被聚1-赖氨酸均聚物,完全取代了PLL-PEG共聚物以暴露出具有蛋白质粘附力的表面。因此,p(TMAEMA- b- MPC)共聚物系统包括可扩展的方法以产生排斥蛋白的表面,而没有表面引发的聚合反应的复杂性并具有聚两性离子的优点。
更新日期:2017-11-14
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