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Noncovalent Interactions

When determining noncovalent interactions, the TriVersa NanoMate enables rapid, inexpensive screening and determination of dissociation constants (Kd) for protein-ligand complexes.

  • Perform reproducible noncovalent interactions protein-ligand screening up to 50 times faster and 100 times less expensive than NMR
  • Nozzle-to-nozzle reproducibility enables the rapid determination of dissociation constants (Kd)

"The stability of the spray from the NanoMate allows us to generate high quality protein-ligand data within a couple of minutes. This data can usually be presented with no post application processing." -- Annick Parent, Sanofi-Aventis, Vitry-sur-Seine

“…we have demonstrated the power of nanoESI-MS…individual oligomeric species within complex mixtures of self-assembling molecules can be identified unambiguously… without the need for prior separation.”
A.S. Ashcroft et al J Mol Biol 2006, xx, xxx-xxx

How it works >>

Following are peer reviewed articles, application notes, and posters demonstrating Advion's technology. You will need to sign in to access the documents listed below.
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Product Notes:

Articles:

  • Determination of active enzyme concentration using activity-based probes and direct mass spectrometric readout
    Ce´dric Bovet, Renato Zenobi
    Analytical Biochemistry 373 (2008) 380–382
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  • Identification of Endocrine-Disrupting Compounds Using Nanoelectrospray Ionization Mass Spectrometry Cédric Bovet, Marc Ruff, Arno Wortmann, Sylvia Eiler, Florence Granger, Bertran Gerrits, Dino Moras, and Renato Zenobi Chimia 62 (2008) 1–6
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  • Which Electrospray-Based Ionization Method Best Reflects Protein-Ligand Interactions Found in Solution? A Comparison of ESI, nanoESI, and ESSI for the Determination of Dissociation Constants with Mass Spectrometry Matthias Conradin Jecklin, David Touboul, Cédric Bovet, Arno Wortmann, and Renato Zenobi J Am Soc Mass Spectrom 2008, 19, 332–343
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  • Binding constant determination of high-affinity protein–ligand complexes by electrospray ionization mass spectrometry and ligand competition
    Arno Wortmann, Matthias C. Jecklin, David Touboul, Martin Badertscher and Renato Zenobi
    J. Mass Spectrom. (2007)
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  • Real-Time Monitoring of Protein Complexes Reveals their Quaternary Organization and Dynamics
    Alexander J. Painter, Nomalie Jaya, Eman Basha, Elizabeth Vierling, Carol V. Robinson, and Justin L.P. Benesch
    Chemistry & Biology 15, 246–253, March 2008
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  • "Estrogen receptor–ligand complexes measured by chip-based nanoelectrospray mass spectrometry: An approach for the screening of endocrine disruptors;" R. Zenobi - ETH Zurich; Protein Science; 3-3-2007
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  • "Direct Observation of Oligomeric Species formed in the Early Stages of Amyloid Fibril Formation using Electrospray Ionisation Mass Spectrometry;" S. Radford - University of Leeds; Journal of Molecular Biology; 11-3-2006
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  • "Monitoring the Zinc Affinity of the Metallo-ß-Lactamase CphA by Automated nanoESI-MS"; Kris De Vriendt et al - University of Ghent; Journal of the American Society for Mass Spectrometry; 1-3-2006
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  • "Real-time Monitoring of Enzymatic DNA Hydrolysis by Electrospray Ionization Mass Spectrometry"; R.H.H. van den Heuvel, et al.; Nucleic Acids Research; 8-3-2005
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  • "Use of a Microchip Device Coupled with Mass Spectrometry for Ligand Screening of a Multi-Protein Target"; Catherine A. Keetch, Helena Hernandez, Alistair Sterling, Mark Baumert, Mark H. Allen, and Carol V. Robinson; Analytical Chemistry; 9-15-2003
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  • "Quantitative Determination of Noncovalent Binding Interactions Using Automated Nanoelectrospray Mass Spectrometry"; Sheng Zhang, Colleen K. Van Pelt, and David B. Wilson; Analytical Chemistry; 7-1-2003
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  • "Automated Nano-Electrospray Mass Spectrometry for Protein-Ligand Screening by Noncovalent Interaction Applied to Human H-FABP and A-FABP"; K. Benkenstock, et.al. - Biovitrum AB; Journal of Biomolecular Screening; 6-3-2003
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Application Notes:

  • Studying RNA - Small Molecule Binding Using Automated Chip-based Nanoelectrospray Mass Spectrometry in Negative Ion Mode
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  • Quantitative Determination of Noncovalent Protein-Ligand Interactions; Automated Chip-based Nanoelectrospray
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Scientific Posters:

  • Automated Nanoelectrospray Mass Spectrometry From a Chip for Protein-Ligand Screening by Noncovalent Interaction Applied to Human H-FABP and A-FABP - K. Benkestock - Biovitrum AB and Royal Institute of Technology
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  • Noncovalent Electrospray Ionization Mass Spectrometry: A Powerful Tool in Drug Discovery - K. Benkestock - Biovitrum
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  • Quantitative Determination of Noncovalent Protein-Ligand Interactions Using Automated Nanoelectrospray Mass Spectrometry - S. Zhang
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