Conformation Change of a Monoclonal Antibody in Real Time, Mimicking Low pH Hold Viral Inactivation

Webinar Length: 1 hour

In this webinar you will learn:

  • How Microfluidic Modulation Spectroscopy (MMS) can be used to monitor, in real time, conformational changes in a monoclonal antibody
  • Introduction to the AQS3pro MMS system from RedShiftBio
  • Characterization of mAb’s in conjunction with viral inactivation testing, enabled by MMS, is critical to understanding the TRUE structure of your drug product in downstream processing.
  • Microfluidic Modulation Spectroscopy provides a reliable platform with increased sensitivity and higher resolution for secondary structure analysis of biotherapeutics.
  • MMS’s automated walk away workflow makes it applicable for screening studies much earlier in the development process.

"I can do the work of a week in a day with the AQS3pro". Steve LaBrenz

While running a viral inactivation (VIN) process, there is typically no sample testing to see if the protein structure is altered at low pH. Samples are tested before and after for information on protein aggregation and chemical degradation, but nothing is performed in real-time to assess changes during the process, in the low pH buffering conditions.

In this webinar, Dr Steven LaBrenz will present a study where the secondary structure is monitored hourly using Microfluidic Modulation Spectroscopy (MMS), in samples split from a single preparation of mAb at low pH. This mimics a VIN low pH hold, showing the significance of MMS to See Change in mAb's.

Microfluidic Modulation Spectroscopy and Protein Higher Order Structure

MMS provides high-resolution structural information, critical to understanding the effects of the purification process on your biotherapeutic drug. Scientists today are challenged in gathering a complete understanding using available techniques. During biomanufacturing, for example, the VIN process, proteins such as monoclonal antibodies, often undergo conformational changes that can alter their secondary structure, leading to critical variations in their overall function. These changes have been historically difficult to detect, as traditional analytical techniques are poor at detecting small differences in protein structure. MMS however, can detect these changes with great sensitivity and accuracy without the need for dilution.



Steven LaBrenz

Steven LaBrenz

Steven LaBrenz is Scientific Director at Janssen R&D - PDMS. A protein chemist, Steven’s experience includes formulation development and process sciences.
Eugene Ma

Eugene Ma

Eugene Ma Chief Technology Officer at RedShiftBio is responsible for technology innovation and technical support across the full range of activities. Prior to RedShiftBio, Eugene was co-founder and CTO at Aegis Lightwave where he developed its Active Thin Film technology from initial concepts to commercial production of the telecom-qualified devices currently being used today in DWDM optical networks.

Some of the questions you'll get the answer to in this webinar;

Have you ever looked at the conformation changes reversed during the neutralization step?

Has RedShiftBio done any work comparing the precision and accuracy of the AQS3pro to a CD spectra device?