Amongst its structural attributes, a protein’s secondary structural features – such as alpha helices, beta sheets, and other conformations – are critical parameters that must be assessed diligently.
Amongst its structural attributes, a protein’s secondary structural features – such as alpha helices, beta sheets, and other 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.
Heilbronn/Dortmund August 2019: 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 structures. 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 comprehensive 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.
Besides the new Fourier-Transform Infrared (FT-IR) spectrometer based secondary structure characterization method approach it is outmost important also to analyze the protein research object with other indicating methods. Learn more from our broad analytical spectrum at www.protagenproteinservices.
About Protagen Protein Services GmbH (PPS):
Protagen Protein Services (PPS) is a world leading CRO and a recognized expert in mass spectrometry methods for analytical services in protein science. Over 20 years of market experience and the comprehensive spectrum of validated analytical methods ensure the highest quality for customers in the pharmaceutical, biotech and life science industry. PPS supports Biosimilar developers with a broad range of analytical methods and consulting in achieving and demonstrating Biosimilarity. For developing new biological entities (NBEs) PPS supports customer approaches by all-in-one-hand service with including full analytical support, complete documentation and outstanding project management to gain market success.
Contact: Tobias Timtner Tel.: +49 7131 74504-0 Marketing Manager Fax: +49 7131 74 504-299 Protagen Protein Services GmbH E-Mail: marketing@
