Surface plasmon resonance/mass spectrometry interface
| Autor: | Erk Tjalling Gedig, Simone Koenig, Nico Dankbar, Jens Grote |
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| Předmět: |
Analyte
Chemistry Elution education Analytical chemistry Cytochromes c Hydrogels Biosensing Techniques Surface Plasmon Resonance Mass spectrometry Laser Analytical Chemistry law.invention chemistry.chemical_compound Matrix-assisted laser desorption/ionization law Desorption Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Surface plasmon resonance Bifunctional |
| Zdroj: | ResearcherID |
| Popis: | A strategy for combining surface plasmon resonance (SPR) biomolecular interaction analysis, and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) is reported. Both techniques are highly complementary but need separate optimization to improve their individual specificity and sensitivity. Sensor surfaces that are optimal for kinetic analysis are not well suited for MALDI-MS and vice versa. In addition, the transfer of analyte from SPR to MS is crucial and often accompanied by sample loss. To address both of these points, a bifunctional SPR fluid cell was constructed where optimized surfaces can be used for binding studies and MS simultaneously with regard to the special need of each technique. The setup guarantees that the SPR and the loading experiment for MS are performed at identical conditions. A removable pin carries the affinity-surface-bound analyte to the mass spectrometer so that handling is minimized, avoiding analyte elution. Functionalized transfer pins can also be used independently of SPR for microaffinity capture-MS. |
| Databáze: | OpenAIRE |
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