Wednesday, November 20 | 14:00 CST / 15:00 JST
Charge heterogeneity in monoclonal antibodies can negatively impact binding affinity and potency, so it is critical to ensure that individual charge variants of biotherapeutic molecules are thoroughly characterized to ensure product quality. Dr. Chris Heger (Bio-Techne) and Dr. Mike Piazza (Nicoya Lifesciences) will illustrate a fast, simple icIEF fractionation and digital SPR workflow that provides in-depth characterization of the charge variants of a therapeutic bispecific antibody (BsAb) Mosunetuzumab and a research-grade biosimilar. Using a combination of the MauriceFlex™ system and Alto™ Digital SPR™, they demonstrate a novel method that utilizes imaged capillary isoelectric focusing (icIEF)-based charge separation and fractionation followed by binding affinity analysis using surface plasmon resonance, offering a robust and efficient approach to evaluating charge variants. Prior LC-MS analysis of the fractions uncovered interesting differences between the two molecules. The speakers will show how the high-purity fractions of both the innovator drug and a research-grade biosimilar were analyzed by SPR for binding studies with their ligands CD3 and CD20, revealing notable differences in binding affinity, particularly between the biosimilar’s acidic peak and ligand CD20.
What you'll learn
- How to set up a simplified workflow that uses (icIEF)-based charge separation and fractionation followed by digital SPR for deeper insights into charge variant binding affinity.
- How leveraging these two benchtop platforms can uncover critical differences between a therapeutic mAb and its biosimilar.
- What additional context can be gained on these charge variant differences using mass spectrometry analysis.
Upcoming webinar
Accelerating insights into changes in binding affinity of biomolecular charge variants using a simple icIEF fractionation and SPR workflow
Low sample consumption
Get full kinetics and
affinity data with only 2 μL of sample
Simplified workflow
Consolidate all analyses
to a single cartridge
Automated assays
Leverage automated assays that reduce time, effort, and cost
ANALYSIS METHOD
Filter libraries based on binding rate and response.
HEAT MAP
See a visual overview of bind/ not-bind status.
GROUP BY
Filter ‘Bind’ candidates for viewing in a sensorgram.
DO NOT INCLUDE
Exclude erroneous data.
CAROUSEL VIEW
Efficiently navigate to the interaction of your choice.
Key features
Crude sample and serum compatibility, low sample volumes, automated assays, and intuitive software make binding characterization easy. Powered by digital microfluidics, Alto is the world’s most user-friendly SPR system — supporting binding kinetics, screening, epitope binning, and quantitation all within a compact, affordable system with a low cost per test.
Upcoming webinar
Accelerating insights into changes in binding affinity of biomolecular charge variants using a simple icIEF fractionation and SPR workflow
Charge heterogeneity in monoclonal antibodies can negatively impact binding affinity and potency, so it is critical to ensure that individual charge variants of biotherapeutic molecules are thoroughly characterized to ensure product quality. Dr. Chris Heger (Bio-Techne) and Dr. Mike Piazza (Nicoya Lifesciences) will illustrate a fast, simple icIEF fractionation and digital SPR workflow that provides in-depth characterization of the charge variants of a therapeutic bispecific antibody (BsAb) Mosunetuzumab and a research-grade biosimilar. Using a combination of the MauriceFlex™ system and Alto™ Digital SPR, they demonstrate a novel method that utilizes imaged capillary isoelectric focusing (icIEF)-based charge separation and fractionation followed by binding affinity analysis using surface plasmon resonance, offering a robust and efficient approach to evaluating charge variants. Prior LC-MS analysis of the fractions uncovered interesting differences between the two molecules. The speakers will show how the high-purity fractions of both the innovator drug and a research-grade biosimilar were analyzed by SPR for binding studies with their ligands CD3 and CD20, revealing notable differences in binding affinity, particularly between the biosimilar’s acidic peak and ligand CD20.
What you'll learn
- How to set up a simplified workflow that uses (icIEF)-based charge separation and fractionation followed by digital SPR for deeper insights into charge variant binding affinity.
- How leveraging these two benchtop platforms can uncover critical differences between a therapeutic mAb and its biosimilar.
- What additional context can be gained on these charge variant differences using mass spectrometry analysis.
Speakers
- Mike Piazza, PhD, Director of Applications Development, Nicoya Lifesciences
- Chris Heger, PhD, Director of Applications Science,
Bio-Techne - Qinan Zhuang, Sales Director, APAC, Nicoya Lifesciences
- Han Su, PhD, Field Applications Scientist, Nicoya Lifesciences
Speakers
- Mike Piazza, PhD, Director of Applications Development, Nicoya Lifesciences
- Chris Heger, PhD, Director of Applications Science,
Bio-Techne - Qinan Zhuang, Sales Director, APAC, Nicoya Lifesciences
- Han Su, PhD, Field Applications Scientist, Nicoya Lifesciences
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