A Multidimensional Analytical Comparison of Remicade and the Biosimilar Remsima

Pisupati K, et al., 89(9):4838-4846, Anal Chem, 2017

Biosimilars are biological drugs that are “equivalent” with regard to quality, efficacy, and safety to an original innovator product. Due to their low market price, biosimilars are much more affordable to patients who want these life-changing treatments. In recent years, biosimilar monoclonal antibodies (mAbs) increasingly earn regulatory approval and prompted a need for the development of rapid approaches to characterize the innovator and biosimilar products, and to identify their clinically relevant differences. Reported herein is a multidimensional analytical comparison of biosimilar mAb, Remsima (RS) and the original innovator product, Remicade (RC). The methods used to evaluate biosimilarity include, mass spectrometry (MS), ion mobility, quantitative peptide mapping, collision-induced unfolding (CIU) analyses, as well as biophysical techniques such as Bio-Layer Interferometry (BLI). The binding affinities of different lots of RC and RS towards FcγIIIa receptor (FcγRIIIa) were assessed by the BLI. A Pall ForteBio BLItz instrument equipped with Protein G (ProG) Biosensor probes was used to perform all BLI assays. ProG sensor tips were immobilized with the RC or RS samples. Subsequently, association and dissociation kinetics of FcγRIIIa was analyzed by immersing the biosensor tips in various concentrations of FcγRIIIa (FcγRIIIa-V158 variant). The experimental results were fitted to a 1:1 binding model. The ka, kd, and KD values were determined for these binding interactions. Overall results of this investigation provide a template for future analytical comparisons of biosimilar mAbs.

Read More