ESSI
ElectroSonic Spray Ionization (ESSI)
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Overview
ElectroSonic Spray
Ionization (ESSI)
Prosolia's ElectroSonic Spray Ionization (ESSI) sources represent a significant improvement over current ESI and nano-ESI technologies. ESSI provides better desolvation performance as compared to traditional electrospray. With ESSI, one finds very clean mass spectra with a narrow charge state distribution (often a single peak) due to the elimination of peak broadening from solvation and adduct formation, as well as an insensitivity to the presence of salts and buffers in the analyzed solution. Additionally, it has been shown that it is relatively "softer" than nanospray for transferring non-covalent complexes into the gas-phase and that the resulting relative intensities of the free and bound ligand represent (to an extent) solution-phase equilibrium. This is particularly important for protein-ligand binding studies. Basically, with ESSI you get:
- Advantages of nanospray but easier to use
- Better desolvation performance the traditional ESI
Refer to the following publication to learn more about the ElectroSonsic Spray Ionization method.
Takáts, Z.; Wiseman, J.M.; Gologan, B.; Cooks, R.G. Electro-sonic Spray Ionization. A Gentle Technique for Generating Folded Proteins and Protein Complexes in the Gas Phase and Studying Ion-Molecule Reactions at Atmospheric Pressure, Anal. Chem., 2004, 76, 4050-4058
Wiseman, J. M.; Takáts, Z.; Gologan, B.; Davisson, V. J.; Cooks, R. G. Direct Characterization of Enzyme-Substrate Complexes by Using Electrosonic Spray Ionization Mass Spectrometry. Angew. Chem. Int. Ed. 2005, 44, 913-916.
Touboul, D.; Jecklin, M.C.; Zenobi, R. Investigation of Deprotonation Reactions on Globular and Denatured Proteins at Atmospheric Pressure by ESSI-MS. JASMS, 2008, 19, 455-466.
Jecklin, M.C.; Touboul, D.; Bovet, C.; Wortmann, A.; Zenobi, R. 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. JASMS, 2008, 19, 332-343.