应用纳米球刻蚀法在自组装膜修饰的硅表面生成中尺度的网状蛋白层

引用本文: SCHLERETH, Andrew NOOMUNA Panae, GAO Pei. 应用纳米球刻蚀法在自组装膜修饰的硅表面生成中尺度的网状蛋白层[J]. 物理化学学报, 2017, 33(4): 810-815. doi: 10.3866/PKU.WHXB201701032 shu

Citation: SCHLERETH, Andrew NOOMUNA Panae, GAO Pei. Mesoscale Protein Patterning on a Self-Assembled Monolayer Coated Silicon Surface through Nanosphere Lithography[J]. Acta Physico-Chimica Sinica, 2017, 33(4): 810-815. doi: 10.3866/PKU.WHXB201701032 shu

应用纳米球刻蚀法在自组装膜修饰的硅表面生成中尺度的网状蛋白层

Department of Chemistry, Eastern Kentucky University, 521 Lancaster Ave, Richmond 40475, KY, USA
基金项目:
美国国立卫生研究院（P20GM103436）和美国国家科学基金会（3048111570-15-153）资助项目

摘要: 在自组装膜修饰的硅表面制备有序的蛋白阵列是研发生物传感器的先决条件之一，因此如何产生有序的表面蛋白阵列一直是生物医药研究方向的前沿。本研究通过应用纳米球刻蚀法在氧化的10-烯基十一烷基三氯硅烷自组装膜修饰的硅表面生成了网状结构溶菌酶蛋白层。网孔的大小（从纳米到微米级别）由表面沉积的纳米球的尺寸来调控。我们利用原子力显微镜和荧光显微镜对样品表面进行了详细表征。结果表明：这种新方法比传统的通过扫描探针在固体表面修饰而聚集溶菌酶蛋白的方法更快捷简便，而且它能够在相对大的硅表面形成网状蛋白层。此外，网孔表面附着具有强吸附活性的羧酸基团层，它可以通过静电吸引或者共价结合来吸附液相中的第二种蛋白分子。

关键词:

English

Mesoscale Protein Patterning on a Self-Assembled Monolayer Coated Silicon Surface through Nanosphere Lithography

Department of Chemistry, Eastern Kentucky University, 521 Lancaster Ave, Richmond 40475, KY, USA
Received Date: 31 October 2016
Revised Date: 02 January 2017
Available Online: 03 January 2017
Fund Project:
The project was supported by National Institute of General Medical Sciences of the National Institutes of Health, USA (P20GM103436) and National Science Foundation, USA (3048111570-15-153).

Abstract: The patterning and immobilization of protein molecules onto functionalized silicon substrate through surface silane chemistry is of interest because protein patterning is an important prerequisite for the development of protein-based diagnostics in biological and medicinal fields. As a model system, mesoscale netty lysozyme arrays were assembled on oxidized undecyltrichlorosilane (UTSox) monolayer coated silicon surface through nanosphere lithography. The size of the arrays ranged from nanometer to micrometer can be easily adjusted by changing the size of nanospheres applied on the surface. By using nanosphere lithography, we are capable of fabricating a regular array of protein islands over centimeter sample regions. The created lysozyme protein patterns were characterized by atomic force microscopy (AFM) and fluorescence microscope, respectively. The analysis has demonstrated that this newly established approach offers a faster and more reliable process to fabricate netty protein arrays over large areas compared to conventional scanning-probe based fabrication methods. Furthermore, the carboxylic acid-terminated layer on surfaces is particularly effective for immobilizing protein molecules through either electrostatic interactions or covalent attachment via imine bonds. Therefore, the negative-toned protein structure on the surface with carboxylic acid groups coated on the bare areas makes it possible to fabricate two types of protein molecules on one surface.

Key words:

1. [1]
  Rosi, N. L.; Mirkin, C. A. Chem. Rev. 2005, 105, 1547. doi: 10.1021/cr030067f
2. [2]
  Ngunjiri, J.; Garno, J. C. Anal. Chem. 2008, 80, 1361. doi: 10.1021/ac086049l
3. [3]
  Christman, K. L.; Enriquez-Rios, V. D.; Maynard, H. D. Soft Matter 2006, 2, 928. doi: 10.1039/b611000b
4. [4]
  Cornell, B. A.; BraachMaksvytis, V. L. B.; King, L. G.; Osman, P. D. J.; Raguse, B.; Wieczorek, L.; Pace, R. J. Nature 1997, 387, 580. doi: 10.1038/42432
5. [5]
  Liu, W.; Li, Y.; Yang, B. Sci. China Chem. 2013, 56, 1087. doi: 10.1007/s11426-013-4909-6.
6. [6]
  Kane, R. S.; Takayama, S.; Ostuni, E.; Ingber, D. E.; Whitesides, G. M. Biomaterials 1999, 20, 2363. doi: 10.1016/S0142-9612(99)00165-9
7. [7]
  Chou, S. Y.; Krauss, P. R.; Renstrom, P. J. J. Vac. Sci. Technol. B 1996, 14, 4129. doi: 10.1116/1.588605
8. [8]
  Hoff, J. D.; Cheng, L. J.; Meyhofer, E.; Guo, L. J.; Hunt, A. J. Nano Lett. 2004, 4, 853. doi: 10.1021/nl049758x
9. [9]
  Lee, K. B.; Park, S. J.; Mirkin, C. A.; Smith, J. C.; Mrksich, M. Science 2002, 295, 1702. doi: 10.1126/science.1067172
10. [10]
  Cheung, C. L.; Camarero, J. A.; Woods, B.W.; Lin, T.W.; Johnson, J. E.; De Yoreo, J. J. J. Am. Chem. Soc. 2003, 125, 6848. doi: 10.1021/ja034479h
11. [11]
  Liu, G. Y.; Amro, N. A. Proc. Natl. Acad. Sci. U. S. A. 2002, 99, 5165. doi: 10.1073/pnas.072695699
12. [12]
  Case, M. A.; McLendon, G. L.; Hu, Y.; Vanderlick, T. K.; Scoles, G. Nano Lett. 2003, 3, 425. doi: 10.1021/nl025795h
13. [13]
  Kenseth, J. R.; Harnisch, J. A.; Jones, V.W.; Porter, M. D. Langmuir 2001, 17, 4105. doi: 10.1021/La0100744
14. [14]
  Pavlovic, E.; Oscarsson, S.; Quist, A. P. Nano Lett. 2003, 3, 779. doi: 10.1021/nl025795h
15. [15]
  Gu, J. H.; Yam, C. M.; Li, S.; Cai, C. Z. J. Am. Chem. Soc. 2004, 126, 8098. doi: 10.1021/ja048405x
16. [16]
  Saner, C. K.; Lu, L.; Zhang, D. H.; Garno, J. C. Nanotechnol. Rev. 2015, 4, 129. doi: 10.1515/ntrev-2015-0002
17. [17]
  Ye, X.; Qi, L. Nano Today 2011, 6, 608. doi: 10.1016/j.nantod.2011.10.002
18. [18]
  Lin, W. F.; Swartz, L. A.; Li, J. R.; Liu, Y.; Liu, G. Y. J. Phys. Chem. C 2013, 117, 23279. doi: 10.1021/jp406239d.
19. [19]
  Taylor, Z. R.; Keay, J. C.; Sanchez, E. S.; Johnson, M. B.; Schmidtke, D.W. Langmuir 2012, 28, 9656. doi: 10.1021/la300806m
20. [20]
  Cai, Y. G.; Ocko, B. M. Langmuir 2005, 21, 9274. doi: 10.1021/la051656e
21. [21]
  Garno, J. C.; Amro, N. A.; Wadu-Mesthrige, K.; Liu, G. Y. Langmuir 2002, 18, 8186. doi: 10.1021/la020518b
22. [22]
  Singh, G.; Griesser, H. J.; Bremmell, K.; Kingshott, P. Adv. Funct. Mater. 2011, 21, 540. doi: 10.1002/adfm.201001340
23. [23]
  Bognar, J.; Szucs, J.; Dorko, Z.; Horvath, V.; Gyurcsanyi, R. E. Adv. Funct. Mater. 2013, 23, 4703. doi: 10.1002/adfm.201300113
24. [24]
  Park, S. J. Korean Phys. Soc. 2015, 67, 706. doi: 10.3938/jkps.67.706
25. [25]
  Dixit, C. K.; Kumar, A.; Kaushik, A. Biochem. Biophys. Res. Commun. 2012, 423, 473. doi: 10.1016/j.bbrc.2012.05.144
26. [26]
  Sun, P.; Xu, L.; Zhao, W. M. Acta Phys. Sin. 2008, 56, 1951. doi: 10.7498/aps.57.1951
27. [27]
  Zhou, Z. T.; Yang, L.; Yao, J. Acta Phys. Sin. 2013, 62, 188104. doi: 10.7498/aps.62.188104
28. [28]
  Tillman, N.; Ulman, A.; Schildkraut, J. S.; Penner, T. L. J. Am. Chem. Soc. 1988, 110, 6136. doi: 10.1021/Ja00226a031
29. [29]
  Wasserman, S. R.; Tao, Y. T.; Whitesides, G. M. Langmuir 1989, 5, 1074. doi: 10.1021/La00088a035
30. [30]
  Gao, P.; Cai, Y. G. Langmuir 2008, 24, 10334. doi: 10.1021/la801020b
31. [31]
  Gao, P.; Cai, Y. G. Ultramicroscopy 2009, 109, 1023. doi: 10.1016/j.ultramic.2009.03.023
32. [32]
  Gershevitz, O.; Sukenik, C. N. J. Am. Chem. Soc. 2004, 126, 482. doi: 10.1021/Ja037610u
33. [33]
  Koehler, J. A.; Ulbricht, M.; Belfort, G. Langmuir 1997, 13, 4162. doi: 10.1021/La970010m
34. [34]
  Faucheux, N.; Schweiss, R.; Lutzow, K.; Werner, C.; Groth, T. Biomaterials 2004, 25, 2721. doi: 10.1016/j.biomaterials.2003.09.069
35. [35]
  Nimura, N.; Kinoshita, T.; Yoshida, T.; Uetake, A.; Nakai, C. Anal. Chem. 1988, 60, 2067. doi: 10.1021/Ac00170a017
36. [36]
  Cai, Y. G. Langmuir 2009, 25, 5594. doi: 10.1021/la9004483

扫一扫看文章

计量

PDF下载量: 1
文章访问数: 836
HTML全文浏览量: 111

通讯作者: 陈斌, bchen63@163.com

1.
沈阳化工大学材料科学与工程学院沈阳 110142

应用纳米球刻蚀法在自组装膜修饰的硅表面生成中尺度的网状蛋白层

English

Mesoscale Protein Patterning on a Self-Assembled Monolayer Coated Silicon Surface through Nanosphere Lithography

CCS Chemistry：嵌段共聚物自组装成 “三明治”二维有机材料，实现纳米级压力传感功能

CCS Chemistry：颜徐州、鲍哲南：你的皮肤可能是一片SPMs

CCS Chemistry：工作高效不疲劳，只须让催化剂动起来

CCS Chemistry：静电组装导向聚合- 聚电解质纳米凝胶量化制备新策略

CCS Chemistry：金黄色葡萄球菌醛基脱氢酶是如何识别特异性底物的？

计量

通讯作者: 陈斌, bchen63@163.com

中国化学会秘书处

应用纳米球刻蚀法在自组装膜修饰的硅表面生成中尺度的网状蛋白层

English

Mesoscale Protein Patterning on a Self-Assembled Monolayer Coated Silicon Surface through Nanosphere Lithography

CCS Chemistry：嵌段共聚物自组装成 “三明治”二维有机材料，实现纳米级压力传感功能

CCS Chemistry：颜徐州、鲍哲南： 你的皮肤可能是一片SPMs

CCS Chemistry：工作高效不疲劳，只须让催化剂动起来

CCS Chemistry：静电组装导向聚合- 聚电解质纳米凝胶量化制备新策略

CCS Chemistry：金黄色葡萄球菌醛基脱氢酶是如何识别特异性底物的？

计量

文章相关

通讯作者: 陈斌, bchen63@163.com

中国化学会秘书处

CCS Chemistry：颜徐州、鲍哲南：你的皮肤可能是一片SPMs