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Whitepaper: BIOshell™ IgG 1000 Å C4 UHPLC column for improved biomacromolecule separations

Posted: 28 June 2018 | | No comments yet

Monoclonal antibodies (mAbs) are widely manufactured by many biopharmaceutical companies to treat a myriad of diseases ranging from Alzheimer’s disease, Parkinson’s disease, ulcerative colitis, and many types of cancers…

Most recombinant therapeutic mAbs belong to the human immunoglobulin G (IgG) category among the immunoglobulin superfamily.

A general IgG antibody is composed of two light chains (LC) that are tethered to two heavy chains (HC) through disulfide bonds. In addition, due to the fact that the LC and HC are composed of amino acids with reactive side chains, IgG’s can be post-translationally modified through phosphorylation, methylation, oxidation, and nitrosylation, among other modifications. These modifications may change the binding affinity of the mAb so that it binds either the wrong antigen, does not bind any antigen, or associates with the wrong cell surface receptor.

Biopharmaceutical companies need to develop rigorous methods to assess lot-to-lot reproducibility of their candidate biologic drug, and the above mentioned modifications are known as Critical Quality Attributes (CQAs) that both the Food and Drug Administration (FDA) and the European Medicines Agency (EMA) monitor. Due to these stringent requirements from regulatory bodies, much research has been pursued in the past 20 years to develop accurate, robust, and high-throughput methods to assess biopharmaceutical purity and structure.

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