New FT–IR Spectrometer Enhances Protagen Protein Services’ Analytical Capabilities

Protagen Protein Services’ (PPS) recently acquired Brucker Tensor II IR spectrometer, which uses Fourier-Transform infrared (FT–IR) spectroscopy technology, significantly enhances the company’s analytical capabilities. The company acquired the new spectrometer in August 2019. Equipped with an AquaSpec transmission cell, the advanced instrument completes and refines the company’s characterization service package by enabling higher order structural characterization as well as providing elaborate results in a relatively short time period.

FT–IR spectroscopy is highly sensitive to the secondary structure of proteins and has been widely used to investigate protein folding. A protein’s secondary structure features-such as alpha helices, beta sheets, and other conformations-are critical parameters that must be assessed diligently.

Comprehensive information on the numerous structural attributes of a protein therapeutic is vital for understanding a protein’s functionality, stability, and antigenicity. FT–IR spectrometers are powerful tools for characterizing the advanced structure of protein-based biologics. They also allow for the monitoring of vibrational modes of the amide bonds within a protein while in its native state and formulation matrix.

While a protein will display many infrared-absorbing bands, amide band I is quite sensitive and representative of the protein conformational states. It is thus 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 Brucker Tensor II IR spectrometer can conduct rapid and sensitive assays with a high degree of throughput and allows for accelerated data acquisition while at the same time requiring low sample amounts. The transmission cell is specially designed to analyze proteins in aqueous solution. The spectrometer’s FT–IR capability can also be used to analyze buffer components (salts, detergents, excipients). While other stability indicating methods such as differential scanning calorimetry, dynamic light scattering, or hydrogen deuterium exchange–mass spectrometry remain substantial for any protein research object’s analysis, this new platform expands PPS’ range of services and completes overall biopharmaceutical characterization, stability and comparability studies, biosimilarity assessment, and formulation development.

Source: Protagen Protein Services