ArticleNature chemistry2025
De novo design of light-responsive protein-protein interactions enables reversible formation of protein assemblies.
Article in Nature chemistry, 2025. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Site-Specific Features Guiding Effective Reversible Photocontrol of Tryptophan Synthase With the Unnatural Amino Acid AzoF.Chembiochem : a European journal of chemical biology · 2026Article
- Photo-Responsive Functional Hydrogels: Mechanism, Design, and Application.Chemistry, an Asian journal · 2026Review
- Redesign of the Ferritin Ferroxidase Center for Universal Molecular Binding or Specific Recognition.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Spatiotemporally programmed tissue regeneration via visible-light-responsive hydrogels: Biosafety-oriented design and applications.Materials today. Bio · 2026Review
- High-performance hydrogels in orthopedics: Structural design, performance tuning, and clinical potential.Materials today. Bio · 2026Review
- Design of miniprotein inhibitors targeting complement C9 to block membrane attack complex assembly.Nature communications · 2026Article
- Precise Regulation of Membrane Proteins: From Physical Technology to Biomolecular Strategy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Optogenetic engineering of synthetic and natural receptors: design principles, functional mechanisms and biomedical applications.Regenerative biomaterials · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors.
Funding
Abstract
Light-responsive proteins play an essential role in all domains of life by sensing and responding to environmental light signals. However, the de novo design of light-responsive proteins with precisely defined structures and reversible responsive behaviours is an unmet challenge. Here we describe a computational approach to design protein-protein interactions regulated by non-canonical amino acids, focusing on the light-responsive phenylalanine-4'-azobenzene (AzoF). Using this approach, we designed light-responsive cyclic homo-oligomers and heterodimers, which only assemble in AzoF's trans configuration and disassemble when AzoF photoisomerizes to the cis configuration. Biophysical characterization confirms the light-responsive assembly and disassembly of these complexes, and the crystal structures match the design models with atomic accuracy. We demonstrate the applicability of these light-responsive proteins in constructing light-responsive hydrogels and engineering synthetic ligand receptors to optocontrol cell signalling in mammalian cells. Our approach opens avenues for designing environmentally responsive protein structures and broadens the toolkit for optogenetics and optochemistry.
Indexed as
Identifiers
40877575What Socratic holds
Registered trials
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 Socratic graph.