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Identification of protein-protein interactions by surface plasmon resonance followed by mass spectrometry
Karolinska Institutet . (CMM - Translational Neuropharmacology)
Karolinska Institutet. (CMM - Translational Neuropharmacology)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences, MMS, Medical Mass Spectrometry.
Karolinska Institutet. (CMM - Translational Neuropharmacology)
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2011 (English)In: Current protocols in protein science, ISSN 1934-3663, Vol. Suppl. 65, 19.21.1-19.21.9 p.Article in journal (Refereed) Published
Abstract [en]

Elucidation of the function and meaning of the protein networks can be useful in the understanding of many pathological processes and the identification of new therapeutic targets. This unit describes an approach to discover protein-protein interactions by coupling surface plasmon resonance to mass spectrometry. Briefly, a protein is covalently bound to a sensor chip, which is then exposed to brain extracts injected over the surface via a microfluidic system. This allows the monitoring in real-time of the interactions between the immobilized ligand and the extracts. Interacting proteins from the extracts are then recovered, trypsinized, and identified using mass spectrometry. The data obtained are searched against a sequence database using the Mascot software. To exclude nonspecific interactors, control experiments using blank sensor chips, and/or randomized peptides, are performed. The protocol presented here does not require specific labeling or modification of proteins and can be performed in <4 days.

Place, publisher, year, edition, pages
2011. Vol. Suppl. 65, 19.21.1-19.21.9 p.
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
URN: urn:nbn:se:uu:diva-166350DOI: 10.1002/0471140864.ps1921s65PubMedID: 21842469OAI: oai:DiVA.org:uu-166350DiVA: diva2:476123
Available from: 2012-01-11 Created: 2012-01-11 Last updated: 2012-01-25Bibliographically approved

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