Characterization of the aggregation propensity of charge variants of recombinant human growth hormone.

Biopharmaceutical products are subject to in depth analysis to ensure and improve their safety and efficacy. As part of this effort the stability and aggregation mechanisms of the therapeutic protein is characterized over the whole life cycle. The stability and aggregation behavior of single charge variants present in biopharmaceuticals were hardly investigated.

Identification of monoclonal antibody variants involved in aggregate formation - Part 2: Hydrophobicity variants.

Monoclonal antibodies (mAbs) are valuable tools both in therapy and in diagnostic. Their tendency to aggregate is a serious concern. Since a mAb drug substance (DS) is composed of different variants, it is important for manufacturers to know the behavior and stability not only of the mAb as a whole, but also of the variants contained in the product.

Identification of monoclonal antibody variants involved in aggregate formation - Part 1: Charge variants.

Biopharmaceutical products contain conformational and chemical variants, that are typically well characterized regarding identity and activity. However, little is known about their self-interaction propensity and tendency to unfold, which are critical characteristics for drug stability and safety. This study aimed to separate and compare charge variants of a monoclonal antibody (mAb) and to identify aggregation prone species.