Using Microfluidic Modulation Spectroscopy to Monitor Protein Misfolds and Structural Similarity
Date: June 27th 2018
Time: 11am ET
Webinar Length: 1 hour
Speakers: Brent Kendrick, VP R&D at Elion Labs and Eugene Ma, CTO at RedShiftBio
Host: Cambridge Healthtech Institute
The R&D department at Elion Labs (a division of KBI Biopharma) is studying analytical capabilities to measure the impact of manufacturing and formulation processes on protein structure. IR and CD spectroscopies are common techniques for this application. They can be used to assess and compare the impact of process changes on protein structure, structural comparisons of drugs made by different manufacturers (e.g. biosimilars), changes in structure that can occur in stored drug formulations, and optimizing protein formulations against structural impurities.
This webinar assesses the detectability of misfolded species by Microfluidic Modulation Spectroscopy (MMS), FTIR and CD spectroscopies using a system from RedShiftBio. An IgG1 drug product, which is predominantly β-sheet, is used to assess misfold detection limits by quantitatively spiking in an α-helical structural impurity. The relative abilities of common spectral data comparison and deconvolution methods to detect misfolds will be discussed.
- How Microfluidic Modulation Spectroscopy (MMS) can be used to study protein secondary structure
- Introduction to the AQS3™pro MMS system from RedShiftBio