ArticleCommunications biology2022
Structure-based rational design of an enhanced fluorogen-activating protein for fluorogens based on GFP chromophore.
Article in Communications 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, 13 citations in OpenAlex.
- Reversible, Chemically Gated FRET via Ligand-Activated Acceptors.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Lifetime-based multiplexed detection of viral RNA using fluorogenic aptamers.bioRxiv : the preprint server for biology · 2026Article
- A color-tailored fluorogenic sensor for hydrogen peroxide.Nature chemical biology · 2026Article
- Bathochromic Shift via C=O to C=S Substitution: A Far-Red Fluorogen for Multiplexed FLIM with FAST Fluorogen-Activating Protein.International journal of molecular sciences · 2025Article
- Fluorescence Lifetime-Based Separation of FAST-Labeled Cellular Compartment.Bio-protocol · 2025Article
- Fluorescence Lifetime Multiplexing with Fluorogen-Activating FAST Protein Variants and Red-Shifted Arylidene-Imidazolone Derivative as Fluorogen.Biosensors · 2025Article
- Monitoring GPCR conformation with GFP-inspired dyes.iScience · 2024Article
- Fluorescence lifetime multiplexing with fluorogen activating protein FAST variants.Communications biology · 2024Article
- A multi-colour fluorogenic tag and its application inMicrobiology (Reading, England) · 2024Article
- Spatial Structure of NanoFAST in the Apo State and in Complex with its Fluorogen HBR-DOM2.International journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
"Fluorescence-Activating and absorption-Shifting Tag" (FAST) is a well-studied fluorogen-activating protein with high brightness and low size, able to activate a wide range of fluorogens. This makes FAST a promising target for both protein and fluorogen optimization. Here, we describe the structure-based rational design of the enhanced FAST mutants, optimized for the N871b fluorogen. Using the spatial structure of the FAST/N871b complex, NMR relaxation analysis, and computer simulations, we identify the mobile regions in the complex and suggest mutations that could stabilize both the protein and the ligand. Two of our mutants appear brighter than the wild-type FAST, and these mutants provide up to 35% enhancement for several other fluorogens of similar structure, both in vitro and in vivo. Analysis of the mutants by NMR reveals that brighter mutants demonstrate the highest stability and lowest length of intermolecular H-bonds. Computer simulations provide the structural basis for such stabilization.
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