Abstract
The similarity between a proposed biosimilar product and the reference product can be affected by many factors. This study is designed to examine whether any subtle difference in the distribution of the charge variants of an Avastin biosimilar can affect its in vitro potency and in vivo PK. Here, the acidic, basic and main peak fractions of a biosimilar product were isolated using high-performance cation-exchange chromatography and were subjected to various studies to compare their in vitro properties and in vivo PK profile. A serial of analytical methods, including size exclusion chromatography (SEC), imaged capillary isoelectric focusing (icIEF) capillary zone electrophoresis (CZE) and cation-exchange chromatography (CEX-HPLC) were also used to characterize the isolated charge variants. The kinetics constant was measured using a Biacore X100 system. The study indicates the biosimilar product has a high similarity with avastin in physicochemical properties. The potency in vitro and PK profile in rat of charge variants and biosimilar product are consistent with avastin.
Highlights
Monoclonal antibodies have become an important class of therapeutic proteins and the fastest growing class of therapeutic agents due to their advantages of being highly specific and relatively homogeneous [1,2,3]
The purity of the charge variants, the biosimilar product and Avastin were determined by the weak cation-exchange method
We have demonstrated that the preparation of the acidic variant, the basic variant and the main peak of the Avastin biosimilar can be achieved by the strong cation exchange method with high purity in terms of charge heterogeneity and size distribution
Summary
Monoclonal antibodies (mAbs) have become an important class of therapeutic proteins and the fastest growing class of therapeutic agents due to their advantages of being highly specific and relatively homogeneous [1,2,3]. As the patents of many original biologics expire, the development of biosimilar products with similar quality, safety and efficacy to the original biologics will improve the accessibility of biotherapeutic drugs to patients. Many regulatory agencies worldwide have already made guidelines to regulate the development of biosimilar products in their countries. Despite their medical advantages, most biologics, especially mAbs, have high molecular weights and complicated structures, posing a challenge to the development of biosimilars. MAb products have heterogeneous variants due to a series of post-translational.
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