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Related Experiment Video

Updated: Jun 3, 2026

Purification and Analytics of a Monoclonal Antibody from Chinese Hamster Ovary Cells Using an Automated Microbioreactor System

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Aggregation stability of a monoclonal antibody during downstream processing.

Paolo Arosio¹, Giuliano Barolo, Thomas Müller-Späth

¹Department of Chemistry and Applied Biosciences Institute for Chemical and Bioengineering, ETH Zurich, 8093 Zurich, Switzerland.

Pharmaceutical Research

|March 31, 2011

Summary

Low pH and salt induce reversible IgG aggregation to small oligomers, affecting protein stability during downstream processing. Aggregation kinetics depend on salt concentration and are modeled by the Lumry-Eyring model.

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Area of Science:

Biochemistry
Protein Chemistry
Pharmaceutical Sciences

Background:

Immunoglobulin G (IgG) stability is critical for downstream processing.
Understanding aggregation kinetics informs process optimization and product quality.

Purpose of the Study:

To investigate the impact of pH and salt concentration on IgG stability and aggregation.
To analyze IgG aggregation kinetics under typical downstream processing conditions.

Main Methods:

Dynamic light scattering (DLS) for aggregate size analysis.
Size exclusion chromatography (SEC) and field flow fractionation (FFF) for oligomer distribution.
Circular dichroism (CD) for monitoring secondary structure changes.

Main Results:

Low pH (<4.0) and salt induce reversible IgG aggregation to oligomers.
Aggregation rate increases with salt concentration, accompanied by increased β-sheet structure.
SEC and FFF successfully characterized oligomer distributions, consistent with Lumry-Eyring model predictions.

Conclusions:

Low pH and salt trigger conformational changes leading to reversible aggregation in IgG.
Under studied conditions, only small soluble oligomers (up to trimers) are formed.
No macroscopic changes were observed, indicating the formation of sub-visible aggregates.