ArticleChembiochem : a European journal of chemical biology2022
A Light-Activatable Photocaged Variant of the Ultra-High Affinity ALFA-Tag Nanobody.
Article in Chembiochem : a European journal of chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Conditionally Activatable Antibody Platforms: Mechanisms, Modalities, and Clinical Translation Potential.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
- A Plug-in system for reprogramming the editing patterns of base editors.Nature communications · 2025Article
- Broad application of the ALFA tagging technology for in planta nanobody-based imaging and biochemical characterization of plant proteins.Plant communications · 2025Article
- Principles and Design of Molecular Tools for Sensing and Perturbing Cell Surface Receptor Activity.Chemical reviews · 2025Review
- Optogenetics with Atomic Precision─A Comprehensive Review of Optical Control of Protein Function through Genetic Code Expansion.Chemical reviews · 2025Review
- The potential of ALFA-tag and tyramide-based fluorescence signal amplification to expand the CRISPR-based DNA imaging toolkit.Journal of experimental botany · 2024Article
- Synthetic Biology Meets CaCells · 2024Review
- Regulation of IL-24/IL-20R2 complex formation using photocaged tyrosines and UV light.Frontiers in molecular biosciences · 2023Article
- Characterization of a Nanobody-Epitope Tag Interaction and Its Application for Receptor Engineering.ACS chemical biology · 2022Article
- A Light-Activatable Photocaged Variant of the Ultra-High Affinity ALFA-Tag Nanobody.Chembiochem : a European journal of chemical biology · 2022Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Nanobodies against short linear peptide-epitopes are widely used to detect and bind proteins of interest (POI) in fusion constructs. Engineered nanobodies that can be controlled by light have found very recent attention for various extra- and intracellular applications. We here report the design of a photocaged variant of the ultra-high affinity ALFA-tag nanobody, also termed ALFA-tag photobody. ortho-Nitrobenzyl tyrosine was incorporated into the paratope region of the nanobody by genetic code expansion technology and resulted in a ≥9,200 to 100,000-fold impairment of the binding affinity. Irradiation with light (365 nm) leads to decaging and reconstitutes the native nanobody. We show the light-dependent binding of the ALFA-tag photobody to HeLa cells presenting the ALFA-tag. The generation of the first photobody directed against a short peptide epitope underlines the generality of our photobody design concept. We envision that this photobody will be useful for the spatiotemporal control of proteins in many applications using cultured cells.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.