Which Electrospray-Based Ionization Method Best Reflects Protein-Ligand Interactions Found in Solution?

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Author(s) Jecklin, Matthias Conradin, Touboul, David, Bovet, Cédric, Wortmann, Arno, Zenobi, Renato
Publication Type Journal Items, Publication Status: Published
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Title Which Electrospray-Based Ionization Method Best Reflects Protein-Ligand Interactions Found in Solution?
Subtitle A Comparison of ESI, nanoESI, and ESSI for the Determination of Dissociation Constants with Mass Spectrometry
Author(s) Jecklin, Matthias Conradin
Touboul, David
Bovet, Cédric
Wortmann, Arno
Zenobi, Renato
Journal or Series Title Journal of the American Society for Mass Spectrometry
Volume Number 19
Issue Number 3
Start Page 332
End Page 343
ISSN 1044-0305
Publisher Springer
Publication Place New York
Publication Date 2008
Abstract We present a comparison of three different electrospray-based ionization techniques for the investigation of noncovalent complexes with mass spectrometry. The features and characteristics of standard electrospray ionization (ESI), chip-based nanoESI, and electrosonic spray ionization (ESSI) mounted onto a hybrid quadrupole time-of-flight mass spectrometer were compared in their performance to determine the dissociation constant (KD) of the model system hen egg white lysozyme (HEWL) binding to N,N′,N″-triacetylchitotriose (NAG3). The best KD value compared with solution data were found for ESSI, 19.4 ± 3.6 μM. Then, we determined the KDs of the two nucleotide binding sites of adenylate kinase (AK), where we obtained KDs of 2.2 ± 0.8 μM for the first and 19.5 ± 8.0 μM for the second binding site using ESSI. We found a weak charge state dependence of the KD for both protein-ligand systems, where for all ionization techniques the KD value decreases with increasing charge state. We demonstrate that ESSI is very gentle and insensitive to instrumental parameters, and the KD obtained is in good agreement with solution phase results from the literature. In addition, we tried to determine the KD for the lymphocyte-specific kinase LCK binding to a kinase inhibitor using nanoESI due to the very low amount of sample available. In this case, we found KD values with a strong charge state dependence, which were in no case close to literature values for solution phase.
DOI 10.1016/j.jasms.2007.11.007
Additional Notes Published online November 19, 2007, Received May 16, 2007, Revised November 8, 2007, Accepted November 8, 2007
Document Type Article
Publication Status Published
Language English
Assigned Organisational Unit(s) 03430
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NEBIS System Number 000541631
Source Database ID PP-40959
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  author = "Jecklin, Matthias Conradin and Touboul, David and Bovet, C{\'{e}}dric and Wortmann, Arno and Zenobi, Renato",
  title = "{W}hich {E}lectrospray-{B}ased {I}onization {M}ethod {B}est {R}eflects {P}rotein-{L}igand {I}nteractions {F}ound in {S}olution?: {A} {C}omparison of {E}{S}{I}, nano{E}{S}{I}, and {E}{S}{S}{I} for the {D}etermination of {D}issociation {C}onstants with {M}ass {S}pectrometry",
  journal = "Journal of the American Society for Mass Spectrometry",
  year = 2008,
  volume = "19",
  number = "3",
  pages = "332--343",

E-Citations record created: Thu, 01 Apr 2010, 22:43:52 CET