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Methionine oxidation of proteins analyzed by affinity capillary electrophoresis in presence of silver(I) and gold(III) ions
Author(s) -
Hutanu Andrei,
Hauser Peter C.,
Moritz Bernd,
Kiessig Steffen,
Noël Aurélie,
Stracke Jan O.,
Wild Markus,
Schwarz Maria A.
Publication year - 2021
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.202000355
Subject(s) - capillary electrophoresis , chemistry , methionine , ion , affinity electrophoresis , chromatography , electrophoresis , analytical chemistry (journal) , biochemistry , amino acid , affinity chromatography , organic chemistry , enzyme
Oxidative damage of biopharmaceuticals during manufacturing and storage is a key concern throughout pharmaceutical development. However, few simple and robust analytical methods are available for the determination of oxidation sites. Here, the potential of affinity capillary electrophoresis (ACE) in the separation of proteins with oxidized methionine (Met) residues is shown. Silver(I) and gold(I) ions have the attribute to selectively form complexes with thioethers over sulfoxides. The addition of these ions to the BGE leads to a selective complexation of Met residues and, thus, to a change of charge allowing separation of species according to the different oxidation states of Met. The mechanisms of these interactions are discussed and binding constants for peptides containing Met with silver(I) are calculated. Additionally, the proposed method can be used as an indicator of oxidative stress in large proteins. The presented technique is easily accessible, economical, and has rapid analysis times, adding new approaches to the analytical toolbox of Met sulfoxide detection.