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Updated: Apr 17, 2026

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
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Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

Published on: April 17, 2017

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Hydrogen/deuterium exchange mass spectrometry applied to IL-23 interaction characteristics: potential impact for

Roxana E Iacob1, Stanley R Krystek, Richard Y-C Huang

  • 1Department of Chemistry and Chemical Biology, Northeastern University, Boston, MA, USA.

Expert Review of Proteomics
|February 26, 2015
PubMed

IL-23 is an important therapeutic target for the treatment of inflammatory diseases. Adnectins are targeted protein therapeutics that are derived from domain III of human fibronectin and have a similar protein scaffold to antibodies. Adnectin 2 was found to bind to IL-23 and compete with the IL-23/IL-23R interaction, posing a potential protein therapeutic. Hydrogen/deuterium exchange mass spectrometry and computational methods were applied to probe the binding interactions between IL-23 and Adnectin 2 and to determine the correlation between the two orthogonal methods. This review summarizes the current structural knowledge about IL-23 and focuses on the applicability of hydrogen/deuterium exchange mass spectrometry to investigate the higher order structure of proteins, which plays an important role in the discovery of new and improved biotherapeutics.

Keywords:
biotherapeuticshydrogen/deuterium exchangeinterleukinsmass spectrometryprotein bindingprotein–protein interactionsstructure

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