Modeling on-column reduction of trisulfide bonds in monoclonal antibodies during protein A chromatography
Autor: | Sanchayita Ghose, Marisa Labanca, Lynn Conley, Rupshika Rajshekaran |
---|---|
Rok vydání: | 2017 |
Předmět: |
0301 basic medicine
Chemical substance medicine.drug_class Sulfides Monoclonal antibody 01 natural sciences Biochemistry Redox Analytical Chemistry law.invention Reaction rate 03 medical and health sciences Affinity chromatography law medicine Cysteine Staphylococcal Protein A Chromatography biology Chemistry 010401 analytical chemistry Organic Chemistry Antibodies Monoclonal General Medicine Recombinant Proteins 0104 chemical sciences 030104 developmental biology Models Chemical biology.protein Recombinant DNA Protein A Oxidation-Reduction Protein Processing Post-Translational |
Zdroj: | Journal of Chromatography A. 1479:81-86 |
ISSN: | 0021-9673 |
Popis: | Trisulfides can be a common post-translational modification in many recombinant monoclonal antibodies. These are a source of product heterogeneity that add to the complexity of product characterization and hence, need to be reduced for consistent product quality. Trisulfide bonds can be converted to the regular disulfide bonds by incorporating a novel cysteine wash step during Protein A affinity chromatography. An empirical model is developed for this on-column reduction reaction to compare the reaction rates as a function of typical operating parameters such as temperature, cysteine concentration, reaction time and starting level of trisulfides. The model presented here is anticipated to assist in the development of optimal wash conditions for the Protein A step to effectively reduce trisulfides to desired levels. |
Databáze: | OpenAIRE |
Externí odkaz: |