ArticleScientific reports2025
Engineering of an Fc-specific monovalent protein G for the light-controlled affinity purification of antibodies.
Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- Overcoming the Limitations of Protein A: Evolution of Bacterial Protein-Based and Synthetic Affinity Ligands for High-Performance IgG Purification.International journal of molecular sciences · 2026Review
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2 authors.
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Abstract
Like other widely applied bacterial surface receptor proteins for immunoglobulins (Igs), such as protein A and protein L, the Ig-binding domain of protein G (ProtG) has dual binding activity. ProtG can independently associate both with the Fc region of an antibody (mAb) and with its Fab and, thus, provoke cross-linking if applied in solution. Indeed, we observed pronounced precipitation activity when using ProtG equipped with the Azo-tag as a small adapter molecule for the light-controlled affinity purification of mAbs. We demonstrate that this undesired precipitation phenomenon follows the classical Heidelberger-Kendall curve. Furthermore, we describe a mutant of ProtG in which Asn478 at the interface with the Fab is replaced by Arg, which results in the effective loss of this secondary binding activity while maintaining high affinity towards the Ig Fc region. ProtG
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