Amongst its structural attributes, a protein’s secondary structure features – such as alpha helices, beta sheets, and others conformations – are critical parameters that must be assessed diligently. FT-IR (Fourier-Transform Infrared) spectroscopy is highly sensitive to the secondary structure of proteins and has been widely used to investigate protein folding.
Comprehensive information on the numerous structural attributes of a protein therapeutic is vital for understanding its functionality, stability, and antigenicity. The Fourier-Transform Infrared (FT-IR) spectrometer is a powerful tool for the advanced structural characterization of protein-based biologics and allows for the monitoring of vibrational modes of the amide bonds within a protein while in its native state and formulation matrix.
New FT-IR spectrometer expands and accelerates Protein Characterization Capabilities
While a protein will display many infrared-absorbing bands, amide band I is quite sensitive and representative of the protein conformational states and is used to discern the relative amounts of different types of secondary structure. Together with circular dichroism, FT-IR is part of a comprehensive platform in the characterization of a biologic's secondary structure profile.
The newly acquired state-of-the-art Brucker Tensor II IR spectrometer is equipped with an AquaSpecTM transmission cell and expands the analytical capabilities of PPS significantly. The advanced instrument completes and refines our characterization package not only by enabling higher order structural characterization but also by providing elaborate results in a relatively short time period.
Most sensitive higher order structural analysis
Conducting rapid and sensitive assays with a high degree of throughput, the spectrometer allows for accelerated data acquisition while at the same time requiring low sample amounts only.The transmission cell is specially designed for the analysis of proteins in aqueous solution. Furthermore, FT-IR can be used for the analysis of buffer components (salts, detergents, excipients). While other stability indicating methods such as DSC,DLS or HDX-mass spectrometry remain substantial for any protein research object’s analysis, the new platform enlarges PPS analytical experts’ range of services and completes overall biopharmaceutical characterization, stability and comparability studies, biosimilarity assessment and formulation development by most sensitive higher order structural analysis.
Learn here more about our broad analytical spectrum