Skip to main content
Log in

Surface Enhanced Resonance of Metal Nano Clusters: A Novel Tool for Proteomics

  • Published:
Journal of Nanoparticle Research Aims and scope Submit manuscript

Abstract

A novel ‘nano’-tool based on metal clusters enables the transduction of changes of biorecognitive binding as well as conformation quantitatively into an optical signal which can be observed directly as a color change of a sensor-chip surface.

Proteins including various enzymes and serum proteins were spotted via micro-arraying onto the chip surface forming monolayer and thin film dots. Multi-layered (up to 300 nm thick) nano-gel-pads were stabilized by photo crosslinking the protein dots with UV-light. By deposition of metal-nano clusters, synthesized via chemical means or sputter coating on top of photo-crosslinked macromolecules an optical resonance effect was obtained.

The response of the novel surface enhanced absorption cluster sensor-chip was transduced spectroscopically in the visible and IR range of the spectrum via an 8 μm resolution reflectance scanner.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Aussenegg F.R. et al., 1995. The metal island coated swelling polymer over mirror system (MICSPOMS): a new principle for measuring ionic strength. Sensors and Actuators B 29, 204–209.

    Google Scholar 

  • Bauer G., F. Pittner & T. Schalkhammer, 1999. Metall nanocluster biosensors. Mikrochimica Acta 131(1–2), 107–114.

    Google Scholar 

  • Bensberg, A., 1997. Swelling and shrinking of polyacid gels. Continuum Mech. Thermodyn. 9, 323–340.

    Google Scholar 

  • Catanzano F. et al., 1998. Circular dichroism study of ribonuclease A mutants containing the minimal structural requirements for dimerization and swapping. Int. J. Biol. Macromol. 23(4), 277–285.

    PubMed  Google Scholar 

  • Evans, D.J. Jr, D.G. Evans, S.S. Kirkpatrick & D.Y. Graham, 1991. Characterization of the Helicobacter pylori urease and purification of its subunits. Microb. Pathog. 10(1), 15–26.

    PubMed  Google Scholar 

  • Fagain C.O., 1995. Understanding and increasing protein stability. Biochim. Biophys. Acta 1252(1), 1–14.

    PubMed  Google Scholar 

  • Frens G., 1973. Preparation of gold dispersions of varying particle size: controlled nucleation for the regulation of the particle size in monodisperse gold suspensions. Nature 241, 20–22.

    Google Scholar 

  • Gladilin A.K. & A.V. Levashov, 1998. Enzyme stability in systems with organic solvents. Biochemi. Mosc. 63(3), 345–356.

    Google Scholar 

  • Johnson W.C., 1999. Analyzing protein circular dichroism spectra for accurate secondary structure. Proteins 35(3), 307–312.

    PubMed  Google Scholar 

  • Klibanov A.M. & A. Zaks, 1985. Enzyme-catalyzed processes in organic solvents. Proc. Natl. Acad. Sci. U.S.A 82(10), 3192–3196.

    PubMed  Google Scholar 

  • Klibanov A.M. & T. Ke, 1998. On enzymatic activity in organic solvents as a function of enzyme history. Biotechnol. Bioeng. 57(6), 746–750.

    PubMed  Google Scholar 

  • Leitner A., Z. Zhao, H. Brunner, F.R. Aussenegg & A. Wokaun, 1993. Optical properties of a metal island film close to a smooth metal surface. Appl. Optics 31, 102–110.

    Google Scholar 

  • Nguyen Q.T., Z. Bendjama, R. Clément & Z. Ping, 1999. Poly(dimethylsiloxane) crosslinked in different conditions. Phys. Chem. Chem. Phys. 1, 2761–2766.

    Google Scholar 

  • Philippopoulos M. & C. Lim, 1999. Exploring the dynamic information content of a protein NMR structure: comparison of a molecular dynamics simulation with the NMR and X-ray structures of Escherichia coli ribonuclease H1. Proteins 36(1), 87–110.

    PubMed  Google Scholar 

  • Schalkhammer T. et al., 1995a. The use of metal-island-coated pH-sensitive swelling polymers for biosensor applications. Sensors and Actuators B 24, 166–172.

    Google Scholar 

  • Schalkhammer T. et al., 1995b. Metal Island Coated Polymer Sensor for Direct Determination of the Volume Effect of Chaotropic Agents. Mikrochim. Acta 121, 259–268.

    Google Scholar 

  • Schalkhammer T. et al., 1995c. New Urea sensor based on a metal island coated ion sensitive swelling polymer device. SPIE 2508, 102–110.

    Google Scholar 

  • Turbett G.R., P.B. Hoj, R. Horne & B.J. Mee, 1992. Purification and characterization of the urease enzymes of Helicobacter species from humans and animals. Infect. Immun. 60(12), 5259–5266.

    PubMed  Google Scholar 

  • Wiese H. & R. Rupaner, 1999. Influence of metal ions on the alkali-swelling behavior of carboxylated acrylic polymer latexes. Colloid Polym. Sci. 277, 372–375.

    Google Scholar 

  • Zerovnik E. et al., 1999. Differences in the effects of TFE on the folding pathways of human stefins A and B. Proteins 36(2), 205–216.

    PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Thomas Schalkhammer.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Mayer, C., Palkovits, R., Bauer, G. et al. Surface Enhanced Resonance of Metal Nano Clusters: A Novel Tool for Proteomics. Journal of Nanoparticle Research 3, 359–369 (2001). https://doi.org/10.1023/A:1012564029052

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1012564029052

Navigation