ArticleNature communications2024
Protein purification with light via a genetically encoded azobenzene side chain.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Light-Activated Molecular Purification (LAMP): A Photo-Responsive Affinity-Chromatography Protocol for Recombinant Protein Purification.Current protocols · 2026Article
- Article
- Article
- 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
- Cyclodextrin-Based Supramolecular Hydrogels in Tissue Engineering and Regenerative Medicine.Molecules (Basel, Switzerland) · 2025Review
- Engineering and Structural Elucidation of a Sac7d-Derived IgG Fc-Specific Affitin and Its Application for the Light-Controlled Affinity Purification of Antibodies.Chembiochem : a European journal of chemical biology · 2025Article
- Innovations and challenges in collagen and gelatin production through precision fermentation.World journal of microbiology & biotechnology · 2025Review
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Affinity chromatography is the method of choice for the rapid purification of proteins from cell extracts or culture supernatants. Here, we present the light-responsive Azo-tag, a short peptide comprising p-(phenylazo)-L-phenylalanine (Pap), whose side chain can be switched from its trans-ground state to the metastable cis-configuration by irradiation with mild UV light. Since only trans-Pap shows strong affinity to α-cyclodextrin (α-CD), a protein exhibiting the Azo-tag selectively binds to an α-CD chromatography matrix under daylight or in the dark but elutes quickly under physiological buffer flow when illuminating the column at 355 nm. We demonstrate the light-controlled single-step purification - termed Excitography - of diverse proteins, including enzymes and antibody fragments, without necessitating competing agents or harsh buffer conditions as normally applied. While affinity chromatography has so far been governed by chemical interactions, introducing control by electromagnetic radiation as a physical principle adds another dimension to this widely applied separation technique.
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