| Literature DB >> 25711416 |
Roxana E Iacob1, Stanley R Krystek, Richard Y-C Huang, Hui Wei, Li Tao, Zheng Lin, Paul E Morin, Michael L Doyle, Adrienne A Tymiak, John R Engen, Guodong Chen.
Abstract
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.Entities:
Keywords: biotherapeutics; hydrogen/deuterium exchange; interleukins; mass spectrometry; protein binding; protein–protein interactions; structure
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Year: 2015 PMID： 25711416 PMCID： PMC4409866 DOI： 10.1586/14789450.2015.1018897
Source DB: PubMed Journal: Expert Rev Proteomics ISSN： 1478-9450 Impact factor: 3.940