Journal
ANALYTICAL AND BIOANALYTICAL CHEMISTRY
Volume 407, Issue 5, Pages 1285-1294Publisher
SPRINGER HEIDELBERG
DOI: 10.1007/s00216-014-8373-8
Keywords
SPR-MS; Biomolecular interaction analysis; Surface plasmon resonance; Mass spectrometry; Biological fluid; alpha-amylase; Lysozyme
Funding
- CNRS
- Evry-Val-d'Essonne University
- Genopole
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Detection of protein biomarkers is of major interest in proteomics. This work reports the analysis of protein biomarkers directly from a biological fluid, human saliva, by surface plasmon resonance imaging coupled to mass spectrometry (SPRi-MS), using a functionalized biochip in an array format enabling multiplex SPR-MS analysis. The SPR biochip presented a gold surface functionalized by a self-assembled monolayer of short poly(ethylene oxide) chains carrying an N-hydroxysuccinimide end-group for the immobilization of antibodies. The experiments were accomplished without any sample pre-purification or spiking with the targeted biomarkers. SPRi monitoring of the interactions, immune capture from the biochip surface, and finally onchip matrix-assisted laser desorption/ionization-MS structural identification of two protein biomarkers, salivary alpha-amylase and lysozyme, were successively achieved directly from saliva at the femtomole level. For lysozyme, the on-chip MS identification was completed by a proteomic analysis based on an on-chip proteolysis procedure and a peptide mass fingerprint.
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