文献类型：期刊文献

英文题名：Protein adsorption resistance of PVP-modified polyurethane film prepared by surface-initiated atom transfer radical polymerization

作者：Yuan, Huihui[1,2];Qian, Bin[1,2];Zhang, Wei[1,2];Lan, Minbo[1,2,3]

机构：[1]E China Univ Sci & Technol, Shanghai Key Lab Funct Mat Chem, Shanghai 200237, Peoples R China;[2]E China Univ Sci & Technol, Res Ctr Anal & Test, Shanghai 200237, Peoples R China;[3]E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2016

卷号：363

起止页码：483

外文期刊名：APPLIED SURFACE SCIENCE

收录：;EI(收录号：20160701940274);WOS:【SCI-EXPANDED(收录号:WOS:000370572400062)】；

基金：This project was sponsored by the National Natural Science Foundation of China (NSFC, contract no. 21304034), and the Science and Technology Commission of Shanghai Municipality (STCSM, contract no. 12nm0501100).

语种：英文

外文关键词：Modified PU film; SI-ATRP; PVP brush; Protein adsorption resistance; Competitive adsorption

摘要：An anti-fouling surface of polyurethane (PU) film grafted with Poly(N-vinylpyrrolidone) (PVP) was prepared through surface-initiated atom transfer radical polymerization (SI-ATRP). And the polymerization time was investigated to obtain PU films with PVP brushes of different lengths. The surface properties and protein adsorption of modified PU films were evaluated. The results showed that the hydrophilicity of PU-PVP films were improved with the increase of polymerization time, which was not positive correlation with the surface roughness due to the brush structure. Additionally, the protein resistance performance was promoted when prolonging the polymerization time. The best antifouling PU-PVP (6.0h) film reduced the adsoption level of bovine serum albumin (BSA), lysozyme (LYS), and brovin serum fibrinogen (BFG) by 93.4%, 68.3%, 85.6%, respectively, compared to the unmodified PU film. The competitive adsorption of three proteins indicated that LYS preferentially adsorbed on the modified PU film, while BFG had the lowest adsorption selectivity. And the amount of BFG on PU-PVP (6.0h) film reduced greatly to 0.08 mu g/cm(2), which was almost one-tenth of its adsorption from the single-protein system. Presented results suggested that both hydrophilicity and surface roughness might be the important factors in all cases of protein adsorption, and the competitive or selective adsorption might be related to the size of the proteins, especially on the non-charged films. (C) 2015 Elsevier B.V. All rights reserved.