ArticleJournal of the American Chemical Society2017
Enzyme-Mediated Directional Transport of a Small-Molecule Walker With Chemically Identical Feet.
Article in Journal of the American Chemical Society, 2017. 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 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.
- Autonomous migration of a phosphate group along glycerol and inositol scaffolds driven by a phosphodiester reaction cycle.Nature chemistry · 2026Article
- [1,n]-Metal migrations for directional translational motion at the molecular level.Nature communications · 2025Article
- Non-equilibrium Steady States in Catalysis, Molecular Motors, and Supramolecular Materials: Why Networks and Language Matter.Journal of the American Chemical Society · 2023Review
- Controllable photomechanical bending of metal-organic rotaxane crystals facilitated by regioselective confined-space photodimerization.Nature communications · 2022Article
- Designing light-driven rotary molecular motors.Chemical science · 2021Review
- Influenza as a molecular walker.Chemical science · 2020Review
- Controlling the preferential motion of chiral molecular walkers on a surface.Chemical science · 2019Article
- Tunable Orthogonal Reversible Covalent (TORC) Bonds: Dynamic Chemical Control over Molecular Assembly.Angewandte Chemie (International ed. in English) · 2019Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We describe a small-molecule "walker" that uses enzyme catalysis to discriminate between the relative positions of its "feet" on a track and thereby move with net directionality. The bipedal walker has identical carboxylic acid feet, and "steps" along an isotactic hydroxyl-group-derivatized polyether track by the formation/breakage of ester linkages. Lipase AS catalyzes the selective hydrolysis of the rear foot of macrocyclized walkers (an information ratchet mechanism), the rear foot producing an (R)-stereocenter at its point of attachment to the track. If the hydrolyzed foot reattaches to the track in front of the bound foot it forms an (S)-stereocenter, which is resistant to enzymatic hydrolysis. Only macrocyclic walker-track conjugates are efficiently hydrolyzed by the enzyme, leading to high processivity of the walker movement along the track. Conventional chemical reagents promote formation of the ester bonds between the walker and the track. Iterative macrocyclization and hydrolysis reactions lead to 68% of walkers taking two steps directionally along a three-foothold track.
Identifiers
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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.