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Journal of Materials Science

, Volume 42, Issue 22, pp 9402–9408 | Cite as

Oriented immobilization of IgG on hydroxylated Si(001) surfaces via protein-A by a multiple-step process based on a self-assembly approach

  • G. DemirelEmail author
  • M. O. Çağlayan
  • B. Garipcan
  • M. Duman
  • E. Pişkin
Article

Abstract

The aim of this study was the oriented immobilization of IgG molecules on the silicon surfaces. A multiple-step procedure was applied for oriented immobilization of IgG in this study. After hydroxylation of the Si(001) surfaces, 3-glycidoxypropyltrimethoxysilane (GPTS) molecules were self-assembled onto these substrates. Dipping time and GPTS concentration were found to be effected by on both layer thicknesses and water-contact angles. 2,2′-(ethylenedioxy)diethylamine (EDA) molecules were then covalently attached to the silicon surface with GPTS molecules. There was no effect of concentration on the formation of EDA molecules on the surfaces, while EDA deposition increased with the dipping time significantly. Imaging ellipsometry and atomic force microscopy (AFM) images exhibited aggregate formation at this step. Protein-A molecules were bound to the free amino groups of EDA molecules on the substrate surface, especially onto the aggregates by using a carbodiimide (i.e., EDAC) as the activating agent. We were able to immobilize IgG molecules in an oriented form onto the protein-A attached surfaces, especially in the regions, where EDA aggregates are located.

Keywords

Contact Angle Silicon Surface Monolayer Formation EDAC Ethylenedioxy 

Notes

Acknowledgements

Authors would like to thank Gökçen Birlik Demirel for theoretical calculations. Gökhan Demirel was supported as a post-doctoral fellow by TÜBİTAK. Prof Erhan Pişkin was supported by Turkish Academy of Sciences as a full member.

References

  1. 1.
    Wnag ZH, Jin G (2003) Anal Chem 75:6119CrossRefGoogle Scholar
  2. 2.
    Lee W, Oh BK, Bae YM, Paek SH, Lee WH, Choi JW (2003) Biosens Bioelectron 19:185CrossRefGoogle Scholar
  3. 3.
    Kanno S, Yanagida Y, Haruyama T, Kobatake E, Aizawa M (2000) J Biotechnol 76:207CrossRefGoogle Scholar
  4. 4.
    Lo YS, Huefner ND, Chan WS, Stevens F, Haris JM, Bebe TP (1999) Langmuir 15:1373CrossRefGoogle Scholar
  5. 5.
    Pei RJ, Hu JM, Hu Y, Zeng Y (1998) J Chem Technol Biotechnol 73:59CrossRefGoogle Scholar
  6. 6.
    Sigal GB, Bamddad C, Barberis A, Strominger J, Whitesides GM (1996) Anal Chem 68:490CrossRefGoogle Scholar
  7. 7.
    Bae YM, Oh BK, Lee W, Lee WH, Choi JW (2005) Biosens Bioelectron 21:103CrossRefGoogle Scholar
  8. 8.
    Lu B, Smyth MR, O’Kennedy R (1996) Analyt 121:29RGoogle Scholar
  9. 9.
    Demirel G, Çaykara T, Akaoğlu B, Çakmak M (2007) Surf Sci (submitted)Google Scholar
  10. 10.
    Aspness DE (1985) In: Palik ED (ed) Handbook of optical constants of solids. Academic Press, Orlando, p. 89CrossRefGoogle Scholar
  11. 11.
    Demirel G, Çağlayan MO, Garipcan B, Duman M, Pişkin E (2007) Mater Sci Eng C (submitted)Google Scholar
  12. 12.
    Kulkarni SA, Mirji SA, Mandale AB, Gupta RP, Vijayamohanan KP (2005) Mater Lett 59:3890CrossRefGoogle Scholar
  13. 13.
    Kinloch AJ, Tan KT, Watts JF (2006) J Adhes 82:1117CrossRefGoogle Scholar
  14. 14.
    Wang A, Tang H, Cao T, Salley SO, Simon Ng KY (2005) J Colloid Interf Sci 291:438CrossRefGoogle Scholar
  15. 15.
    Li A, Yang F, Ma Y, Yang X (2007) Biosens Bioelectron 22:1716CrossRefGoogle Scholar
  16. 16.
    Zhang F, Srinivasan MP (2004) Langmuir 20:2309CrossRefGoogle Scholar
  17. 17.
    Yang JH, Song KS, Zhang GJ, Degawa M, Sasaki Y, Ohdomari I, Kawarada H (2006) Langmuir 22:11245CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2007

Authors and Affiliations

  • G. Demirel
    • 1
    Email author
  • M. O. Çağlayan
    • 1
  • B. Garipcan
    • 1
  • M. Duman
    • 1
  • E. Pişkin
    • 1
  1. 1.Department of Chemical Engineering and Division of BioengineeringHacettepe UniversityAnkaraTurkey

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