Proteins suffer oxidative and photolytic degradation via a manifold of radical and non-radical pathways, which lead to a great variety of oxidation products. Analyses of these products and degradation pathways have been optimized, such that they can be applied to almost any proteins, e.g. smaller proteins (< 100 kDa), IgG1 and IgG2 (ca. 150 kDa), and membrane proteins.
Over the last 20+ years, the Schöneich laboratory has characterized many oxidation pathways, identified and quantified novel oxidation and rearrangement products, and started to correlate the reactivity of individual amino acids in proteins with protein structure. Depending on the oxidation conditions (i.e., formulation and storage conditions) of a protein, literally every amino acid can be a target for oxidation.
- Analytical characterization and quantification of protein oxidation products derived from all 20 amino acids present in proteins
- Quantitative analysis and identification of oxidation products in soluble proteins, membrane proteins, and protein aggregates
- Analytical characterization and quantification of photochemical degradation products derived from the 20 amino acids present in proteins
- Quantitative analysis and identification of photochemical degradation products in soluble proteins, membrane proteins, and protein aggregates
- Oxidative and photochemical degradation of proteins in solution and in the solid state (including the determination of quantum yields for photochemical pathways)
- Quantification and characterization of oxidative and photolytic protein aggregation and fragmentation.
Publications: Link to PubMed for Christian Schöneich
Link to Schöneich Department Web page
Dr. Christian Schöneich
Department of Pharmaceutical Chemistry
University of Kansas
2095 Constant Ave
Lawrence, KS 66047