ArticleChembiochem : a European journal of chemical biology2025
Engineering and Structural Elucidation of a Sac7d-Derived IgG Fc-Specific Affitin and Its Application for the Light-Controlled Affinity Purification of Antibodies.
Article in Chembiochem : a European journal of chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers 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
- Structural Basis of the Light-Switchable Interaction between an Azobenzene Side Chain in a Biosynthetic Protein and α-Cyclodextrin.ChemistryOpen · 2026Article
- Engineering of an Fc-specific monovalent protein G for the light-controlled affinity purification of antibodies.Scientific reports · 2025Article
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8 authors.
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Abstract
While protein A affinity chromatography is widely established for antibody purification, the acidic elution conditions often lead to protein aggregation and deamidation. Here, an alternative approach is described for the purification of antibodies utilizing an engineered binding protein based on the archaebacterial Sac7d scaffold in combination with light-controlled α-CD affinity chromatography (Excitography). Starting from a published affitin molecule, a monomeric protein version (C3A24) was engineered by substituting the unpaired thiol side chain Cys24 within the binding site by Ala, and, unexpectedly, its binding activity towards the human IgG1 Fc region was even improved (K
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