ArticleACS synthetic biology2023
Robust Photocontrol of Elastin-like Polypeptide Phase Transition with a Genetically Encoded Arylazopyrazole.
Article in ACS synthetic biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 17 citations in OpenAlex.
- Boosting Reversible Photocontrol of a Photoxenase by an Engineered Conformational Shift.Angewandte Chemie (International ed. in English) · 2026Article
- Expanding the Repertoire of Photoswitchable Unnatural Amino Acids for Enzyme Engineering.Angewandte Chemie (International ed. in English) · 2025Article
- Azobenzene-Modified Temperature-Responsive Short Elastin-like Peptides for Photo-Controlled Phase Transition.ACS synthetic biology · 2025Article
- Reversible Substrate-Specific Photocontrol of the Chemotherapeutic Asparaginase(-Glutaminase) fromACS catalysis · 2025Article
- Optogenetics with Atomic Precision─A Comprehensive Review of Optical Control of Protein Function through Genetic Code Expansion.Chemical reviews · 2025Review
- Programmability and biomedical utility of intrinsically-disordered protein polymers.Advanced drug delivery reviews · 2024Review
- Evolution of Pyrrolysyl-tRNA Synthetase: From Methanogenesis to Genetic Code Expansion.Chemical reviews · 2024Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The rational design of light-responsive proteins and protein-based polymers requires both a photoswitch with suitable light-responsive properties and the ability to incorporate it at (multiple) defined positions in the protein chain. This Letter describes the evolution of high-performance aminoacyl-tRNA synthetases for recognizing a photoswitchable arylazopyrazole-bearing unnatural amino acid (AAP-uAA), which we then incorporated at multiple sites within elastin-like polypeptides (ELPs). The incorporation of AAP-uAA into ELPs yielded proteins capable of an isothermal, reversible, and robust light-mediated soluble-to-insoluble phase transition, which occurred faster (after only 1 min of light irradiation) and demonstrated a larger transition temperature difference (up to a 45 °C difference in the ELP transition temperature upon a cis to trans AAP isomerization) than similar azobenzene-containing ELPs. The evolved translation machinery can be used for the multisite incorporation of AAP at the polypeptide level; moreover, it constitutes a general methodology for designing light-responsive proteins and protein-based polymers with robust light-responsive behavior, made possible by the superior photoswitchable properties of AAP.
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