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  Differential binding studies applying functional protein microarrays and surface plasmon resonance

Seitz, H., Hutschenreiter, S., Hultschig, C., Zeilinger, C., Zimmermann, B., Kleinjung, F., et al. (2006). Differential binding studies applying functional protein microarrays and surface plasmon resonance. PROTEOMICS, 6(19), 5132-5139. doi:10.1002/pmic.200500181.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-8392-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-8393-9
Genre: Journal Article

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 Creators:
Seitz, Harald1, Author              
Hutschenreiter, Silke, Author
Hultschig, Claus2, Author
Zeilinger, Carsten, Author
Zimmermann, Bastian, Author
Kleinjung, Frank, Author
Schuchhardt, Johannes, Author
Eickhoff, Holger, Author
Herberg, Friedrich W., Author
Affiliations:
1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              
2Max Planck Society, ou_persistent13              

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Free keywords: Binding studies; Protein microarray; Protein-protein interaction; S100 proteins; Surface plasmon resonance studies
 Abstract: A variety of different in vivo and in vitro technologies provide comprehensive insights in protein-protein interaction networks. Here we demonstrate a novel approach to analyze, verify and quantify putative interactions between two members of the S100 protein family and 80 recombinant proteins derived from a proteome-wide protein expression library. Surface plasmon resonance (SPR) using Biacore technology and functional protein microarrays were used as two independent methods to study protein-protein interactions. With this combined approach we were able to detect nine calcium-dependent interactions between Arg-Gly-Ser-(RGS)-His6 tagged proteins derived from the library and GST-tagged S100B and S100A6, respectively. For the protein microarray affinity-purified proteins from the expression library were spotted onto modified glass slides and probed with the S100 proteins. SPR experiments were performed in the same setup and in a vice-versa approach reversing analytes and ligands to determine distinct association and dissociation patterns of each positive interaction. Besides already known interaction partners, several novel binders were found independently with both detection methods, albeit analogous immobilization strategies had to be applied in both assays.

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Language(s): eng - English
 Dates: 2006-10
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 312999
DOI: 10.1002/pmic.200500181
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Title: PROTEOMICS
Source Genre: Journal
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Pages: - Volume / Issue: 6 (19) Sequence Number: - Start / End Page: 5132 - 5139 Identifier: ISSN: 1615-9853