ArticleProceedings of the National Academy of Sciences of the United States of America2022
Functional enzyme-polymer complexes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers, 1 of them a synthesis that pooled it.
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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
10 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Atomistic-Level Insights into the Role of Mutations in the Engineering of PET Hydrolases: A Systematic Review.International journal of molecular sciences · 2025Pooled it
- NIR-II photothermal-amplified triple catalysis of a spherical mesoporous iron single-atom nanozyme for potentiating ferroptosis-based tumor therapy.Journal of nanobiotechnology · 2026Article
- Computational design of functional random heteropolymers through atomistic simulations.PloS one · 2026Article
- Seeking Precise Protein-like Functions from Random Heteropolymer Ensemble and through Dimensionality Reduction.ACS central science · 2025Review
- Designing single-polymer-chain nanoparticles to mimic biomolecular hydration frustration.Nature chemistry · 2025Article
- Sequence-Sensitivity in Functional Synthetic Polymer Properties.Angewandte Chemie (International ed. in English) · 2025Article
- Article
- Selectivity of Complex Coacervation in Multi-Protein Mixtures.bioRxiv : the preprint server for biology · 2024Article
- Supra-biological performance of immobilized enzymes enabled by chaperone-like specific non-covalent interactions.Nature communications · 2024Article
- Rheology and Gelation of Hyaluronic Acid/Chitosan Coacervates.Biomolecules · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
SignificanceThe use of biological enzyme catalysts could have huge ramifications for chemical industries. However, these enzymes are often inactive in nonbiological conditions, such as high temperatures, present in industrial settings. Here, we show that the enzyme PETase (polyethylene terephthalate [PET]), with potential application in plastic recycling, is stabilized at elevated temperature through complexation with random copolymers. We demonstrate this through simulations and experiments on different types of substrates. Our simulations also provide strategies for designing more enzymatically active complexes by altering polymer composition and enzyme charge distribution.
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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 OpenQuestion graph.