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Feasibility of polyelectrolyte-driven Fab fragment separation.

Florian Capito¹, Harald Kolmar, Bianca Edelmann

¹Institute for Organic Chemistry and Biochemistry, Technische Universität Darmstadt, Darmstadt, Germany; Merck KGaA, PTD, Darmstadt, Germany. florian.capito@external.merckgroup.com.

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Summary

A novel copolymer effectively separates therapeutic antigen-binding fragments (Fabs) from monoclonal antibodies (mAbs) and fragment constant regions (Fcs). This method leverages differential precipitation for simpler purification of Fabs, meeting rising demand.

Keywords:

Antibodies Downstream processing Polymers Protein purification

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Area of Science:

Biotechnology
Protein Chemistry
Bioseparations

Background:

Therapeutic antigen-binding fragments (Fabs) require efficient purification methods.
Existing purification strategies for Fabs can be complex and costly.
Monoclonal antibodies (mAbs) and fragment constant regions (Fcs) are common contaminants.

Purpose of the Study:

To evaluate the feasibility of using a copolymer for separating Fabs from mAbs and Fcs.
To investigate the physicochemical basis for differential protein precipitation.
To explore a simplified purification strategy for therapeutic Fabs.

Main Methods:

Utilized a copolymer with both hydrophobic and anionic properties.
Tested protein precipitation yields in blended solutions of Fabs, mAbs, and Fcs.
Analyzed protein hydrophobicity using 2-p-toluidinonaphthalene-6-sulfonate.

Main Results:

The copolymer efficiently precipitated mAbs and Fcs via combined electrostatic and hydrophobic interactions.
Fabs showed reduced precipitation yields, primarily driven by electrostatic interactions sensitive to ionic strength.
Hydrophobicity analysis confirmed Fcs > mAbs > Fabs.

Conclusions:

The copolymer demonstrates selective precipitation of Fabs from mAbs and Fcs.
Differential physicochemical properties underpin the separation mechanism.
This approach offers a potentially simpler purification strategy for therapeutic Fabs.