Temperature-modulated adsorption of poly(N-isopropylacrylamide)-grafted ferritin on solid substrate

被引:3
|
作者
Kumashiro, Yoshikazu [1 ]
Ikezoe, Yasuhiro [3 ]
Hayashi, Tomohiro [2 ,3 ]
Okabayashi, Youichi [3 ,4 ]
Tamada, Kaoru [5 ]
Yamato, Masayuki [1 ]
Okano, Teruo [1 ]
Hara, Masahiko [2 ,3 ,4 ]
机构
[1] Tokyo Womens Med Univ TWIns, Inst Adv Biomed Engn & Sci, Shinjuku Ku, Tokyo 1628666, Japan
[2] Tokyo Inst Technol, Interdisciplinary Grad Sch Sci & Engn, Dept Elect Chem, Midori Ku, Yokohama, Kanagawa 2268502, Japan
[3] RIKEN Adv Sci Inst, Flucto Order Funct Res Team, RIKEN HYU Collaborat Res Ctr, Wako, Saitama 3510198, Japan
[4] Hanyang Univ, Flucto Order Funct Res Team, RIKEN HYU Collaborat Res Ctr, Fus Technol Ctr 5F, Seoul 133791, South Korea
[5] Kyushu Univ, Inst Mat Chem & Engn, Higashi Ku, Fukuoka 8128581, Japan
关键词
Protein adsorption; Temperature-responsive polymer; Protein-polymer conjugate; Hydrophobic interaction; THERMORESPONSIVE POLYMERS; PROTEIN; SURFACES; CAGE; NANOPARTICLES; MONOLAYERS; ARRAY;
D O I
10.1016/j.colsurfb.2012.02.028
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Ferritin grafted with temperature-responsive poly(N-isopropylacrylamide) (PIPAAm-ferritin) was synthesized by a coupling reaction using PIPAAm and ferritin for obtaining stimuli-responsive biomaterials. The hydrodynamic diameter of PIPAAm-ferritins in aqueous solution increased at 37 degrees C at a higher protein concentration (>0.2 mg/mL) because of the intermolecular aggregation through the hydrophobic interaction of PIPAAm chains. On the other hand. PIPAAm-ferritins at a lower concentration (<0.2 mg/mL) were unable to increase their size even at 37 degrees C. The adsorption kinetics of PIPAAm-ferritins on hydrophobically modified Si substrate were evaluated with a quartz crystal microbalance in 10 mmol/L Bis-Tris/HCl buffer (pH 5.8) with and without poly(oxyethylene) sorbitan monolaurate (TWEEN 20) (0.05 wt%) as a surfactant. Although the adsorption of PIPAAm-ferritins on hydrophobic Si substrate at 25 degrees C in the buffer with TWEEN 20 was hardly observed. PIPAAm-ferritins were considerably adsorbed on the substrate at 37 degrees C, indicating that the hydrophobic interaction between the substrate and PIPAAm grafts on the ferritins after the destruction of the hydrophobic interaction between the protein and the substrate by TWEEN 20. (C) 2012 Elsevier B.V. All rights reserved.
引用
收藏
页码:57 / 64
页数:8
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