Advancing Structural Characterization of Therapeutic Proteins Using MMS

18 Jul, 2022 | Newsletters
Advancing Structural Characterization of Therapeutic Proteins Using MMS
Existing tools for measuring and monitoring the structure of biotherapeutic molecules during formulation have, until now, had very significant limitations in sensitivity and ease of use. 

In this webinar, we share data that demonstrates the power of Microfluidic Modulation Spectroscopy (MMS), a valuable, fully-automated IR technology, to generate high-quality, reproducible secondary structure data for protein therapeutics, including monoclonal antibodies. 

Learning Objectives: 
•    How Amgen obtained high-quality structural data on low concentration mAbs to enable more confident decision-making in the formulation process
•    How to detect previously undetectable structural changes in therapeutic proteins to profoundly affect quality control outcomes using MMS 
•    The fundamentals of Microfluidic Modulation Spectroscopy and advantages over existing techniques


RedShiftBio’s structural analysis instrument, the AQS³pro and Apollo, provides users with the ability to measure critical changes in bimolecular structure.  AQS³pro overcomes many of the limitations of traditional spectroscopy-based technologies, with ultrasensitive, highly reproducible, automated structural measurements of proteins and other biomolecules.    

Measuring Buffer-Induced Structural Changes in a Beta-sheet Rich Protein using MMS
In this study, the structural differences of alpha-chymotrpysin, a beta-sheet rich protein, were characterized in water and three common formulation buffers using MMS. Alphachymotrypsin was prepared in HPLC-grade water as a reference, as well as in Phosphate Buffer (PB), Phosphate Buffered Saline (PBS), and Tris buffer. Absorption spectra in the Amide I region were automatically collected and processed to monitor critical structural components including the beta-sheet content, HOS motif percentages, and to calculate the overall structural similarities between samples in all prepared conditions. The resulting analysis and comparison across all buffer conditions show that alpha-chymotrypsin undergoes buffer-induced structural changes.