@article{Dragusanu2010Onlin-1091,
  year={2010},
  doi={10.1016/j.jasms.2010.06.011},
  title={On-line bioaffinity-electrospray mass spectrometry for simultaneous detection, identification, and quantification of protein-ligand interactions},
  number={10},
  volume={21},
  issn={1044-0305},
  journal={Journal of The American Society for Mass Spectrometry},
  pages={1643--1648},
  author={Drăguşanu, Mihaela and Petre, Brînduşa-Alina and Slamnoiu, Stefan and Vlad, Camelia and Tu, Tingting and Przybylski, Michael and Dragusanu, Mihaela}
}

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    <dcterms:title>On-line bioaffinity-electrospray mass spectrometry for simultaneous detection, identification, and quantification of protein-ligand interactions</dcterms:title>
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    <dc:contributor>Petre, Brînduşa-Alina</dc:contributor>
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    <dc:creator>Vlad, Camelia</dc:creator>
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    <dcterms:abstract xml:lang="eng">We describe here an on-line combination of a surface acoustic wave (SAW) biosensor with electrospray ionization mass spectrometry (SAW-ESI-MS) that enables the direct detection,identification, and quantification of affinity-bound ligands from a protein ligand complex on a biosensor chip. A trapping column was used between the SAW-biosensor and the electrospray mass spectrometer equipped with a micro-guard column, which provides simultaneous sample concentration and desalting for the mass spectrometric analysis of the dissociated ligand. First applications of the on-line SAW-ESI-MS combination include (1), differentiation of â-amyloid (Aâ) epitope peptides bound to anti-Aâ antibodies; (2), the identification of immobilized Substance P peptide calmodulin complex; (3), identification and quantification of the interaction of 3-nitrotyrosine-modified peptides with nitrotyrosine-specific antibodies; and (4), identification of immobilized anti-á-synuclein human á-synuclein complex. Quantitative determinations of protein ligand complexes by SAW yielded dissociation constants (KD) from micro-to low nanomolar sample concentrations. The on-line bioaffinity-ESI-MS combination presented here is expected to enable broad bioanalytical application to the simultaneous, label-free determination and quantification of biopolymer-ligand interactions, as diverse as antigen-antibody and lectin-carbohydrate complexes.</dcterms:abstract>
    <dcterms:bibliographicCitation>First publ. in: Journal of The American Society for Mass Spectrometry 21 (2010), 10,  pp. 1643-1648</dcterms:bibliographicCitation>
    <dc:contributor>Vlad, Camelia</dc:contributor>
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    <dc:creator>Drăguşanu, Mihaela</dc:creator>
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    <dc:creator>Przybylski, Michael</dc:creator>
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    <dc:contributor>Drăguşanu, Mihaela</dc:contributor>
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    <dc:creator>Petre, Brînduşa-Alina</dc:creator>
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    <dc:creator>Slamnoiu, Stefan</dc:creator>
    <dc:contributor>Przybylski, Michael</dc:contributor>
    <dc:creator>Tu, Tingting</dc:creator>
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