Scientific Article: Use of Maurice CE-SDS in ICH Q6B based Biosimilar Comparability Exercises

The biosimilars market is a hugely significant sector of the biopharmaceutical industry with long-term, significant growth projections. The main attraction for manufacturers to produce biosimilars is the decreased time to market, owing to a more abbreviated pathway to regulatory approval. The route to market places strong emphasis on the analytical and characterization techniques used to investigate the structure of the molecule and, most importantly, side-by-side comparability exercises between the biosimilar and innovator products.

Both the EMA and FDA have set out clear guidelines for companies aiming to produce biosimilars, including the expectations for analytical investigation into structure. In these documents, the EMA and FDA both cite ICH Q6B as the guideline for biosimilar testing and highlight the need for using orthogonal techniques that enable cross-verification of data and conclusions from different methodologies.

While no specific methods for analytical assessment of electrophoretic patterns are noted in the document, recommendations of analytical approaches are suggested to fulfil each expectation and are caveated by phrases such as “or other suitable procedures.” A newer technique that improves upon the standard gel electrophoresis approach is capillary gel electrophoresis. In this technique, proteins within a sample are separated in a gel-filled capillary based on their electrophoretic mobility, which in turn is determined by each protein’s charge and size. When subjected to an electric field, proteins of different sizes migrate at different velocities, and this migration is detected by methods such as UV absorbance, fluorescence and mass spectrometry.

Maurice™ and Maurice S. are two of the platforms available for fully automated and highly quantitative capillary electrophoresis-sodium dodecyl sulphate (CE-SDS) analysis. The studies presented in this article demonstrate the utility of Maurice platforms in biosimilar development through the characterization of certain monoclonal antibodies, heavily glycosylated species, and PEGylated species.