ArticleProtein science : a publication of the Protein Society2021
Structure-based design of a photoswitchable affibody scaffold.
Article in Protein science : a publication of the Protein Society, 2021. 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.
- Affibody Complex Formation: An In-Depth Thermodynamic Analysis Using Isothermal Titration Calorimetry.Molecules (Basel, Switzerland) · 2026Article
- Conditionally Activatable Antibody Platforms: Mechanisms, Modalities, and Clinical Translation Potential.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
- A Yeast Two-Hybrid Assay to Develop Optogenetic Tools for Controlling Protein-Protein Interactions.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Effects of binding partners on thermal reversion rates of photoswitchable molecules.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Design of a light and CaProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Lighting up yeast: overview of optogenetics in yeast and their applications to yeast biotechnology.FEMS yeast research · 2025Review
- Enhancing response of a protein conformational switch by using two disordered ligand binding domains.Frontiers in molecular biosciences · 2023Article
- Light-regulated gene expression in Bacteria: Fundamentals, advances, and perspectives.Frontiers in bioengineering and biotechnology · 2022Review
- Combinatorial Approaches for Efficient Design of Photoswitchable Protein-Protein Interactions asFrontiers in bioengineering and biotechnology · 2022Article
- Structure-based design of a photoswitchable affibody scaffold.Protein science : a publication of the Protein Society · 2021Article
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Abstract
Photo-control of affinity reagents offers a general approach for high-resolution spatiotemporal control of diverse molecular processes. In an effort to develop general design principles for a photo-controlled affinity reagent, we took a structure-based approach to the design of a photoswitchable Z-domain, among the simplest of affinity reagent scaffolds. A chimera, designated Z-PYP, of photoactive yellow protein (PYP) and the Z-domain, was designed based on the concept of mutually exclusive folding. NMR analysis indicated that, in the dark, the PYP domain of the chimera was folded, and the Z-domain was unfolded. Blue light caused loss of structure in PYP and a two- to sixfold change in the apparent affinity of Z-PYP for its target as determined using size exclusion chromatography, UV-Vis based assays, and enyzme-linked immunosorbent assay (ELISA). A thermodynamic model indicated that mutations to decrease Z-domain folding energy would alter target affinity without loss of switching. This prediction was confirmed experimentally with a double alanine mutant in helix 3 of the Z-domain of the chimera (Z-PYP-AA) showing >30-fold lower dark-state binding and no loss in switching. The effect of decreased dark-state binding affinity was tested in a two-hybrid transcriptional control format and enabled pronounced light/dark differences in yeast growth in vivo. Finally, the design was transferable to the αZ-Taq affibody enabling tunable light-dependent binding both in vitro and in vivo to the Z-Taq target. This system thus provides a framework for the focused development of light switchable affibodies for a range of targets.
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