Surface plasmon resonance-enabled mass spectrometry arrays
Biosensors that utilize surface plasmon resonance (SPR) as a method of detection of protein interactions can be used for selective separation of proteins prior to MS analysis. The combination of SPR and MS results in a unique multiplexed detection technology capable of both quantitative and qualitat...
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Published in | Electrophoresis Vol. 27; no. 18; pp. 3671 - 3675 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Weinheim
WILEY-VCH Verlag
01.09.2006
WILEY‐VCH Verlag |
Subjects | |
Online Access | Get full text |
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Summary: | Biosensors that utilize surface plasmon resonance (SPR) as a method of detection of protein interactions can be used for selective separation of proteins prior to MS analysis. The combination of SPR and MS results in a unique multiplexed detection technology capable of both quantitative and qualitative protein analysis. To further the development of a high‐throughput SPR‐MS approach, the possibility of arraying binding ligands on SPR chips for affinity capture of proteins and their MS analysis was explored. Antibodies to β‐2‐microglobulin, cystatin C, transferrin, and insulin‐like growth factors I and II were arrayed on a large number of SPR chips. Human plasma samples were injected over the antibody array chips in an SPR Biosensor, after which on‐chip MS analysis was performed to detect the bound proteins. Signals from the targeted proteins were observed for each antibody‐derivatized chip, indicating successful antibody immobilization and protein capture. The SPR‐MS arrays are robust, highly reproducible, and are capable of high‐throughput analysis. |
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Bibliography: | ArticleID:ELPS200600065 istex:74C364BB43505EFD9705C6926A99DFD98CFBAEC7 ark:/67375/WNG-DF4WXGQL-0 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0173-0835 1522-2683 |
DOI: | 10.1002/elps.200600065 |