Comparing Microfluidic Modulation Spectroscopy (MMS), FTIR and Circular Dichroism Spectroscopy for Detecting Protein Misfolds & Structural Similarity
New Whitepaper from RedShiftBio
A protein misfold represents a structural impurity and at any level can result in changed efficacy and increase the potential for immunogenicity. Measuring low level impurities in secondary structure is necessary to maintain confidence in a protein's integrity during all phases of drug development. FTIR and Circular Dichroism (CD) are commonly used for this, but have known limitations in reproducibility and sensitivity. Microfluidic Modulation Spectroscopy (MMS) is a new protein characterization method which generates reproducible high resolution measurements, directly addressing the shortcomings of FTIR and CD.
This whitepaper from RedShiftBio directly compares the three techniques.
The lab used BSA spiked into IgG1 as this mimics a ‘best-case' ability to detect a very different structural impurity (IgG1 is mainly ß-sheet, while BSA is mainly a-helix). This whitepaper demonstrates that MMS out-performs traditional FTIR and CD methods across a number of parameters.
MMS is a novel spectroscopic technique that combines a microfluidic cell and a mid-IR laser to rapidly scan and accurately detect and measure change in protein misfolding and similarity in secondary structure.