Antibody-Antigen Complex Structure
Biosimilars Structure Characterization
The three-dimensional structure is a strong contributor to the acceleration of any therapeutics program and provides clear and indisputable data for patent applications. X-ray crystallographic structures of antigen-antibody complexes are essential for elucidating the details of epitope-paratope interactions and for optimizing the binding interactions in the complex. We at SARomics Biostructures have gathered extensive experience in antibody:antigen complex and biosimilars higher order structure (HOS) characterization, which includes biophysical characterization in solution, crystallization and X-ray structure determination (see our case study below) as well as NMR spectroscopy studies. Our crystallography services and NMR spectroscopy platforms ncludes all necessary equipment and tools for handling projects of this type.
Testing, analysis and validation of higher order structures of biosimilars is critical to the development of products that adhere to patient safety principles. SARomics Biostructures offers a multidisciplinary approach for the best possible comparability assessment and analysis of HOS at atomic resolution. By combining NMR spectroscopy and X-ray crystallography, we can provide both global structural information and detailed atomic position analysis, which will detect any differences in the structures of the samples.
Our biosimilars testing and analysis services are based on recent revolutionary advances in NMR spectroscopy that have made it possible without expensive isotope labeling to acquire a unique fingerprint representation of the 3D conformation of large, complex molecules like biologics. By directly matching the NMR fingerprint of a given protein to its high-resolution 3D structure, e.g. determined by X-ray crystallography, or to a fingerprint of another protein batch or a biosimilar, we can rapidly assess and analyze comparability and show that the molecules, for example a biosimilar and its originator, or different batches or alternative preparations of the same biologic, have identical higher order structure.