Case Studies
Benefits of our FTIR services
Our FTIR expertise has already been used to solve a wide range of complex customer challenges from structural characterization and glycan analysis to in-process monitoring. See below for more details of how our techniques have been used in real-world situations.
Colloidal aluminium salts such as aluminum hydroxide are routinely used to improve antigen immunogenicity. Adsorption affects protein conformation in a range of different ways, and can increase or decrease its stability, depending on its physicochemical properties. Therefore, analyzing the protein in this adsorbed state is crucial, but very challenging due to the scattering properties of the adjuvant, so most of the methods currently used require a desorption step. We used our expertise in fourier-transform infrared (FTIR) spectroscopy, to develop a methodology to monitor protein stability is its adsorbed state, without desorption.
Biosimilar development is generating growing interest in the pharmaceutical sector as many biological drug patents fall into the public domain. However, biosimilars are very complex to characterize and highly sensitive to minor changes in manufacturing conditions, requiring additional methods to compare their critical quality attributes, safety and efficacy with the reference product. We combined our expertise in fourier-transform infrared (FTIR) spectroscopy with statistical tools to develop a rapid and reliable method to compare secondary structure and glycan composition of batches of biosimilar candidates with their respective references (originators).
Glycosylation is the most common post-translational modification (PTM) in proteins, especially in biopharmaceuticals. It is a critical quality attribute with a wide range of impacts on factors, including such as product stability, bioactivity and safety. However, current glycan analysis methods involve multiple and lengthy sample preparation steps which can affect the robustness of the analyses. Therefore, the development of an orthogonal, direct and simple method is necessary. We demonstrated that fourier-transform infrared (FTIR) spectroscopy is capable of distinguishing two monoclonal antibodies with highly similar glycan composition.
Glycosylation is the most common post-translational modification (PTM) in proteins, especially in biopharmaceuticals. It is a critical quality attribute with a wide range of impacts on factors, including such as product stability, bioactivity and safety. However, current glycan analysis methods involve multiple and lengthy sample preparation steps which can affect the robustness of the analyses. Therefore, the development of an orthogonal, direct and simple method is necessary. Using fourier-transform infrared (FTIR) spectroscopy, we demonstrated that the intensity of a specific region of the spectrum clearly increases with global glycosylation level.
In recent years, virus-like particles (VLP) have emerged as a safe and effective advanced vaccine platform. However, the characterization of VLP preparations remains a challenge, due to their large size, diversity and complexity. Fourier transform infrared (FTIR) spectroscopy can be used to compare the protein structure and the lipid and protein ratio of VLPs and can, therefore, be used as a tool to monitor the quality control of VLP-based vaccines.
The 1H / 2H exchange kinetic provides information about protein conformation, since the exchange rate depends on the stability of the secondary structure and on the accessibility of the peptide bond to the aqueous environment. It is an efficient way to compare the tertiary structure of proteins in several experimental conditions. We have demonstrated that FTIR spectroscopy can effectively monitor hydrogen-deuterium exchange to compare the protein structure and conformation under two distinct storage conditions.
Tween 20 and 80 are commonly used in biotherapeutic formulations due to their low toxicity and good biocompatibility. However, quantifying them still represents an analytical challenge. We used our expertise in fourier-transform infrared (FTIR) spectroscopy, to develop a methodology to detect and quantify Tween in biopharmaceutical products.