National Institute of Standards and Technology (NIST) researchers at the Institute for Bioscience and Biotechnology Research (IBBR) have demonstrated the most precise method yet to measure the structural configuration of monoclonal antibodies, an important factor in determining the safety and efficacy of these biomolecules as medicines.
Monoclonal antibodies (mAbs) are proteins manufactured in the laboratory that can target specific disease cells or antigens (proteins that trigger an immune reaction) for removal from the body. The method described in a recent paper1 may soon help manufacturers and regulators better assess and compare the performance and quality of mAbs.
Monoclonal antibodies can be used as extremely specific therapeutic agents, including ones designed to target cancer cells unique to an individual. However, in order to properly function as a biotherapeutic agent, the molecule’s structural units — amino acids — must fold into a three-dimensional structure that aligns its active regions with corresponding receptor sites on a target cell or antigen. If “misfolding” occurs, a potent and safe treatment may become ineffective, or worse, provoke a dangerous or fatal immune reaction.
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