Protein adsorption on poly(N-isopropylacrylamide)-modified silicon surfaces: Effects of grafted layer thickness and protein size

被引:88
|
作者
Yu, Qian [1 ]
Zhang, Yanxia [1 ]
Chen, Hong [1 ]
Wu, Zhaoqiang [1 ]
Huang, He [1 ]
Cheng, Chi [1 ]
机构
[1] Wuhan Univ Technol, Sch Mat Sci & Engn, State Key Lab Adv Technol Mat Synth & Proc, Wuhan 430070, Hubei, Peoples R China
关键词
Poly(N-isopropylacrylamide); Thermoresponsive; Thickness; Surface-initiated atom transfer radical polymerization; Protein adsorption; Protein size; TRANSFER RADICAL POLYMERIZATION; BOVINE SERUM-ALBUMIN; SELF-ASSEMBLED MONOLAYERS; MOLECULAR-WEIGHT; BRUSH SURFACES; POLYMERS; LYSOZYME; SYSTEMS; PLASMA; CHAIN;
D O I
10.1016/j.colsurfb.2009.12.006
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
In this work, we investigated the protein adsorption on the end-tethered thermoresponsive poly(N-isopropylacrylamide) (PNIPAAm) brushes with varying grafted layer thickness prepared via surface-initiated atom transfer radical polymerization (SI-ATRP) on initiator-immobilized silicon surfaces. The thickness Of a grafted layer was modulated by adjusting reaction time and/or solvent composition. The surface properties as a function of thickness were investigated by water contact angle, X-ray photoelectron spectroscopy (XPS), and atomic force microscope (AFM). The influence of PNIPAAm-grafted layer thickness on human serum albumin (HSA) adsorption in phosphate-buffered saline (PBS) (pH 7.4) at different temperature was evaluated using a radiolabeling method. In a lower thickness range (< 15 nm), protein adsorption on PNIPAAm-grafted layer shows a thermoresponsive change in a certain extent, but the variation is not remarkable. However, it is interesting to observe that these surfaces exhibit good protein-resistant property. For the surface with a PNIPAAm thickness of 13.4 nm, the HSA adsorption level measured at room temperature was similar to 7 ng/cm(2), corresponding to a reduction of 97% compared to the unmodified silicon surface. For thicker PNIPAAm-grafted surface with thickness of 38.1 nm, the adsorption results of three proteins (HSA, fibrinogen, and lysozyme) with different sizes and charges indicate that the PNIPAAm-modified surface exhibits a size-sensitive property of protein adsorption. (C) 2009 Elsevier B.V. All Fights reserved.
引用
收藏
页码:468 / 474
页数:7
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