Hostname: page-component-745bb68f8f-s22k5 Total loading time: 0 Render date: 2025-02-04T14:31:35.554Z Has data issue: false hasContentIssue false
  • English
  • Français

Attenuation of Protein Adsorption on Static and Vibrating Magnetic Nanowires

Published online by Cambridge University Press:  01 February 2011

Kristy M. Ainslie ,
Gaurav Sharma ,
Maureen A. Dyer ,
Craig A. Grimes  and
Michael V. Pishko
Kristy M. Ainslie
Affiliation:
Materials Research Institute, Department of Chemical Engineering
Gaurav Sharma
Affiliation:
Department of Materials Science and Engineering
Maureen A. Dyer
Affiliation:
Materials Research Institute, Department of Chemical Engineering
Craig A. Grimes
Affiliation:
Department of Materials Science and Engineering Department of Electrical Engineering
Michael V. Pishko
Affiliation:
Materials Research Institute, Department of Chemical Engineering Department of Materials Science and Engineering Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802
Get access

Abstract

The research described here investigates the hypothesis that nanoarchitecture contained in a nanowire array is capable of attenuating the adverse host response, biofouling, generated when medical devices, such as sensors, are implanted in the body. This adverse host response generates an avascular fibrous mass transfer barrier between the device and the analyte of interest, disabling the sensor. Numerous studies have indicated that surface chemistry and architecture modulated the host response. These findings lead us to hypothesize that nanostructured surfaces will significantly inhibit the formation of an avascular fibrous capsule. We are investigating whether vibrating magnetostrictive nanowires, formed in nanowire arrays, can prevent protein and cell adhesion. Magnetostrictive nanowires are fabricated by electroplating a ferromagnetic metal alloy into the pores of a nanoporous alumina template. The ferromagnetic nanowires are made to vibrate by altering the magnetic field surrounding the wires. Enzyme-linked immunosorbent assay (ELISA) and other protein assays were used to study protein adhesion on the nanowire arrays. These results display a reduced protein adhesion per surface area of static nanowires. The vibrating nanowires show a further reduction in protein adhesion, compared to static wires. Studies were also preformed to investigate the effects of nanoarchitecture have on cell adhesion. These studies were performed with both static and vibrating nanowires. Preliminary protein adhesion studies have shown that a nanowire arrays modulate protein adhesion in vitro.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 877: Symposium S – Magnetic Nanoparticles and Nanowires , 2005 , S8.4
Copyright
Copyright © Materials Research Society 2005

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

[1] Padera, R. F., Colton, C. K., Biomaterials 17 (1996) 277–284.Google Scholar
[2] Lampin, M., Warocquier, C., Legris, C., Degrange, M., Sigot-Luizard, M. F., J Biomed Mater Res 36 (1997) 99–108.Google Scholar
[3] Masuda, H., Fukuda, K., Science 268 (1995) 1466–1468.Google Scholar
[4] Zeng, H., Zheng, M., Skomski, R., Sellmyer, D. J., Liu, Y., Menon, L., Bandyopadhyay, S., Magnetic properties of self-assembled Co nanowires of varying length and diameter, in: '(Ed.)'^'(Eds.)', vol 87, AIP, 2000, p.^pp. 4718–4720.Google Scholar
[5] Li, A.-P., Muller, F., Birner, A., Nielsch, K., Gosele, U., Advanced Materials 11 (1999) 483–487.Google Scholar
[6] Osaka, T., Takai, M., Hayashi, K., Ohashi, K., Saito, M., Yamada, K., Nature 392 (1998) 796–798.Google Scholar
[7] Tabakovic, I., Riemer, S., Inturi, V., Jallen, P., Thayer, A., Journal of The Electrochemical Society 147 (2000) 219–226.Google Scholar
[8] Liu, X., Zangari, G., Shen, L., Electrodeposition of soft, high moment Co--Fe--Ni thin films, in: '(Ed.)'^'(Eds.)', vol 87, AIP, 2000, p.^pp. 5410–5412.Google Scholar
[9] Sharma, G., Grimes, C., J Mater Res 19 (2004) 3695.Google Scholar
[10] Jessensky, O., Muller, F., Gosele, U., Applied Physics Letters 72 (1998) 1173–1175.Google Scholar
[11] Norde, W., Macromol Symp 103 (1996) 5–18.Google Scholar
[12] Gau, H., Herminghaus, S., Lenz, P., Lipowsky, R., Science 283 (1999) 46–49.Google Scholar
[13] Abbott, N. L., Folkers, J. P., Whitesides, G. M., Science 257 (1992) 1380.Google Scholar
[14] Lenz, P., Adv. Mater 11 (1999) 1531.Google Scholar
[15] Oner, D., McCarthy, T., Langmuir 16 (2000) 7777–7782.Google Scholar
[16] Feng, L., Li, S., Li, H., Zhai, J., Song, Y., Jiang, L., Zhu, D., Agnew Chem Int Ed 41 (2002) 1221–1223.Google Scholar
[17] Borgs, C., Coninck, J. De, Kotecky, R., Zinque, M., Phys Rev Lett 74 (1995) 2292–2294.Google Scholar