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SGS combines biophysical techniques with more sensitive orthogonal approaches to provide you with a comprehensive view of secondary and tertiary protein structures in a biopharmaceutical formulation.

Life Science

Generating a stable environment for a biopharmaceutical drug product is a critical step for ensuring a long product shelf-life. In order to maintain potency and activity, some of the most critical parameters to maintain are protein conformation (tertiary or 3D structure), folding (secondary structure) and proper subunit association (quaternary structure). Collectively, these are known as higher-order structure (HOS) and can be highly influenced by the formulation environment, manufacturing process and storage conditions.

However, analytical monitoring of the protein conformation has been frequently omitted due to time constraints, the complexity of techniques commonly employed and the inherent lack of sensitivity to subtle changes shown by some biophysical methods.

We offer traditional biophysical techniques, combined with more sensitive orthogonal approaches, to provide you with a comprehensive view of HOS in biopharmaceutical formulation.

Biophysical analysis has become increasingly important in the characterization of biopharmaceutical drug candidates and the analyses used may be described as covering a mixture of disciplines, essentially being the use of physical techniques to investigate and characterize biological systems.

We offer a wide range of analyses for the elucidation of 3D protein structure, including the application of spectroscopic, thermodynamic and hydrodynamic techniques, such as:

  • Circular dichroism (CD)
  • Fourier transform infra-red (FT-IR) spectroscopy
  • Differential scanning calorimetry (DSC)
  • Intrinsic and extrinsic fluorescence
  • Dynamic light scattering (DLS)
  • Size exclusion chromatography multi-angle light scattering (SEC-MALS) 
  • Sedimentation velocity analytical ultracentrifugation (SV-AUC).

By analyzing these properties, we can provide you with valuable information on secondary, tertiary and quaternary structures of protein molecules, such as monoclonal antibodies, and provide evidence that the molecule maintains conformational stability.

To gain accurate analysis of your secondary and tertiary protein structure, contact us today.